eF-site/Summary 5n6l-AB

eF-site ID	5n6l-AB
PDB Code	5n6l
Chain	A, B

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Title	Structure of the membrane integral lipoprotein N-acyltransferase Lnt C387A mutant from E. coli
Classification	TRANSFERASE
Compound	Apolipoprotein N-acyltransferase
Source	(LNT_ECOLI)

Sequence	A:	FASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLM GLQALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATF GGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWL RVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKG LAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLF ALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQL LNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLK ALDGELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGKG APYSYESADRYNKNHLVPFGEFVPLESILRPLAPFFDLPM SSFSRGPYIQPPLSANGIELTAAIAYEIILGEQVRDNFRP DTDYLLTISNDAWFGKSIGPWQHFQMARMRALELARPLLR STNNGITAVIGPQGEIQAMIPQFTREVLTTNVTPTTGLTP YARTGNWPLWVLTALFGFAAVLMSLR
	B:	FASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLM GLQALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATF GGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWL RVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKG LAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLF ALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQL LNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLK ALDGELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGKG APYSYESADRYNKNHLVPFGEFVPLESFSRGPYIQPPLSA NGIELTAAIAYEIILGEQVRDNFRPDTDYLLTISNDAWFG KSIGPWQHFQMARMRALELARPLLRSTNNGITAVIGPQGE IQAMIPQFTREVLTTNVTPTTGLTPYARTGNWPLWVLTAL FGFAAVLMSLR

Description

Functional site


1)	chain	A
	residue	22
	type
	sequence	A
	description	binding site for residue OLC A 601
	source	: AC1

2)	chain	A
	residue	25
	type
	sequence	T
	description	binding site for residue OLC A 601
	source	: AC1

3)	chain	A
	residue	26
	type
	sequence	L
	description	binding site for residue OLC A 601
	source	: AC1

4)	chain	A
	residue	31
	type
	sequence	Y
	description	binding site for residue OLC A 601
	source	: AC1

5)	chain	A
	residue	70
	type
	sequence	S
	description	binding site for residue OLC A 601
	source	: AC1

6)	chain	A
	residue	73
	type
	sequence	N
	description	binding site for residue OLC A 601
	source	: AC1

7)	chain	A
	residue	8
	type
	sequence	E
	description	binding site for residue OLC A 602
	source	: AC2

8)	chain	A
	residue	13
	type
	sequence	R
	description	binding site for residue OLC A 602
	source	: AC2

9)	chain	A
	residue	20
	type
	sequence	F
	description	binding site for residue OLC A 602
	source	: AC2

10)	chain	A
	residue	46
	type
	sequence	A
	description	binding site for residue OLC A 602
	source	: AC2

11)	chain	A
	residue	47
	type
	sequence	L
	description	binding site for residue OLC A 602
	source	: AC2

12)	chain	A
	residue	49
	type
	sequence	F
	description	binding site for residue OLC A 602
	source	: AC2

13)	chain	A
	residue	50
	type
	sequence	N
	description	binding site for residue OLC A 602
	source	: AC2

14)	chain	A
	residue	121
	type
	sequence	W
	description	binding site for residue OLC A 603
	source	: AC3

15)	chain	A
	residue	178
	type
	sequence	M
	description	binding site for residue OLC A 603
	source	: AC3

16)	chain	A
	residue	182
	type
	sequence	L
	description	binding site for residue OLC A 603
	source	: AC3

17)	chain	A
	residue	191
	type
	sequence	N
	description	binding site for residue OLC A 603
	source	: AC3

18)	chain	A
	residue	197
	type
	sequence	V
	description	binding site for residue OLC A 603
	source	: AC3

19)	chain	A
	residue	190
	type
	sequence	R
	description	binding site for residue OLC A 604
	source	: AC4

20)	chain	A
	residue	191
	type
	sequence	N
	description	binding site for residue OLC A 604
	source	: AC4

21)	chain	A
	residue	195
	type
	sequence	L
	description	binding site for residue OLC A 604
	source	: AC4

22)	chain	A
	residue	10
	type
	sequence	Q
	description	binding site for residue OLC A 605
	source	: AC5

23)	chain	A
	residue	14
	type
	sequence	L
	description	binding site for residue OLC A 605
	source	: AC5

24)	chain	A
	residue	52
	type
	sequence	R
	description	binding site for residue OLC A 605
	source	: AC5

25)	chain	A
	residue	55
	type
	sequence	Q
	description	binding site for residue OLC A 605
	source	: AC5

26)	chain	A
	residue	61
	type
	sequence	F
	description	binding site for residue OLC A 605
	source	: AC5

27)	chain	A
	residue	488
	type
	sequence	N
	description	binding site for residue OLC A 606
	source	: AC6

28)	chain	A
	residue	489
	type
	sequence	W
	description	binding site for residue OLC A 606
	source	: AC6

29)	chain	A
	residue	492
	type
	sequence	W
	description	binding site for residue OLC A 606
	source	: AC6

30)	chain	A
	residue	11
	type
	sequence	R
	description	binding site for residue OLC A 607
	source	: AC7

31)	chain	A
	residue	18
	type
	sequence	L
	description	binding site for residue OLC A 607
	source	: AC7

32)	chain	A
	residue	65
	type
	sequence	F
	description	binding site for residue OLC A 607
	source	: AC7

33)	chain	A
	residue	137
	type
	sequence	F
	description	binding site for residue OLC A 608
	source	: AC8

34)	chain	A
	residue	170
	type
	sequence	E
	description	binding site for residue OLC A 608
	source	: AC8

35)	chain	A
	residue	488
	type
	sequence	N
	description	binding site for residue OLC A 608
	source	: AC8

36)	chain	A
	residue	492
	type
	sequence	W
	description	binding site for residue OLC A 608
	source	: AC8

37)	chain	A
	residue	208
	type
	sequence	L
	description	binding site for residue OLC A 609
	source	: AC9

38)	chain	A
	residue	213
	type
	sequence	W
	description	binding site for residue OLC A 609
	source	: AC9

39)	chain	A
	residue	485
	type
	sequence	R
	description	binding site for residue OLC A 609
	source	: AC9

40)	chain	A
	residue	341
	type
	sequence	F
	description	binding site for residue OLC A 610
	source	: AD1

41)	chain	A
	residue	361
	type
	sequence	P
	description	binding site for residue OLC A 610
	source	: AD1

42)	chain	A
	residue	18
	type
	sequence	L
	description	binding site for residue OLC A 611
	source	: AD2

43)	chain	A
	residue	73
	type
	sequence	N
	description	binding site for residue OLC A 611
	source	: AD2

44)	chain	A
	residue	76
	type
	sequence	Y
	description	binding site for residue OLC A 611
	source	: AD2

45)	chain	A
	residue	94
	type
	sequence	V
	description	binding site for residue OLC A 611
	source	: AD2

46)	chain	A
	residue	79
	type
	sequence	I
	description	binding site for residue OLC A 612
	source	: AD3

47)	chain	A
	residue	97
	type
	sequence	L
	description	binding site for residue OLC A 612
	source	: AD3

48)	chain	A
	residue	339
	type
	sequence	V
	description	binding site for residue OLC A 612
	source	: AD3

49)	chain	A
	residue	341
	type
	sequence	F
	description	binding site for residue OLC A 612
	source	: AD3

50)	chain	A
	residue	416
	type
	sequence	F
	description	binding site for residue OLC A 612
	source	: AD3

51)	chain	A
	residue	82
	type
	sequence	F
	description	binding site for residue OLC A 613
	source	: AD4

52)	chain	A
	residue	341
	type
	sequence	F
	description	binding site for residue OLC A 613
	source	: AD4

53)	chain	A
	residue	415
	type
	sequence	W
	description	binding site for residue OLC A 613
	source	: AD4

54)	chain	A
	residue	141
	type
	sequence	W
	description	binding site for residue OLC A 614
	source	: AD5

55)	chain	A
	residue	26
	type
	sequence	L
	description	binding site for residue OLC A 615
	source	: AD6

56)	chain	A
	residue	30
	type
	sequence	P
	description	binding site for residue OLC A 615
	source	: AD6

57)	chain	A
	residue	31
	type
	sequence	Y
	description	binding site for residue OLC A 615
	source	: AD6

58)	chain	A
	residue	356
	type
	sequence	P
	description	binding site for residue OLC A 615
	source	: AD6

59)	chain	A
	residue	196
	type
	sequence	V
	description	binding site for residue OLC A 616
	source	: AD7

60)	chain	A
	residue	200
	type
	sequence	V
	description	binding site for residue OLC A 616
	source	: AD7

61)	chain	A
	residue	203
	type
	sequence	A
	description	binding site for residue OLC A 616
	source	: AD7

62)	chain	A
	residue	497
	type
	sequence	L
	description	binding site for residue OLC A 616
	source	: AD7

63)	chain	A
	residue	197
	type
	sequence	V
	description	binding site for residue OLC A 617
	source	: AD8

64)	chain	A
	residue	201
	type
	sequence	L
	description	binding site for residue OLC A 617
	source	: AD8

65)	chain	A
	residue	204
	type
	sequence	L
	description	binding site for residue OLC A 617
	source	: AD8

66)	chain	A
	residue	146
	type
	sequence	F
	description	binding site for residue OLC A 618
	source	: AD9

67)	chain	A
	residue	339
	type
	sequence	V
	description	binding site for residue OLC A 618
	source	: AD9

68)	chain	A
	residue	340
	type
	sequence	P
	description	binding site for residue OLC A 618
	source	: AD9

69)	chain	A
	residue	54
	type
	sequence	L
	description	binding site for residue OLC A 619
	source	: AE1

70)	chain	B
	residue	211
	type
	sequence	I
	description	binding site for residue OLC A 619
	source	: AE1

71)	chain	B
	residue	212
	type
	sequence	Q
	description	binding site for residue OLC A 619
	source	: AE1

72)	chain	A
	residue	258
	type
	sequence	G
	description	binding site for residue GOL A 620
	source	: AE2

73)	chain	A
	residue	259
	type
	sequence	K
	description	binding site for residue GOL A 620
	source	: AE2

74)	chain	A
	residue	261
	type
	sequence	S
	description	binding site for residue GOL A 620
	source	: AE2

75)	chain	A
	residue	292
	type
	sequence	G
	description	binding site for residue GOL A 620
	source	: AE2

76)	chain	A
	residue	141
	type
	sequence	W
	description	binding site for residue GOL A 621
	source	: AE3

77)	chain	A
	residue	143
	type
	sequence	L
	description	binding site for residue GOL A 621
	source	: AE3

78)	chain	A
	residue	144
	type
	sequence	T
	description	binding site for residue GOL A 622
	source	: AE4

79)	chain	A
	residue	346
	type
	sequence	P
	description	binding site for residue GOL A 622
	source	: AE4

80)	chain	A
	residue	347
	type
	sequence	L
	description	binding site for residue GOL A 622
	source	: AE4

81)	chain	A
	residue	92
	type
	sequence	F
	description	binding site for residue GOL A 623
	source	: AE5

82)	chain	A
	residue	9
	type
	sequence	R
	description	binding site for residue GOL A 624
	source	: AE6

83)	chain	A
	residue	10
	type
	sequence	Q
	description	binding site for residue GOL A 624
	source	: AE6

84)	chain	A
	residue	202
	type
	sequence	F
	description	binding site for residue GOL A 627
	source	: AE9

85)	chain	A
	residue	206
	type
	sequence	F
	description	binding site for residue GOL A 627
	source	: AE9

86)	chain	B
	residue	22
	type
	sequence	A
	description	binding site for residue OLC B 601
	source	: AF1

87)	chain	B
	residue	26
	type
	sequence	L
	description	binding site for residue OLC B 601
	source	: AF1

88)	chain	B
	residue	31
	type
	sequence	Y
	description	binding site for residue OLC B 601
	source	: AF1

89)	chain	B
	residue	70
	type
	sequence	S
	description	binding site for residue OLC B 601
	source	: AF1

90)	chain	B
	residue	73
	type
	sequence	N
	description	binding site for residue OLC B 601
	source	: AF1

91)	chain	A
	residue	86
	type
	sequence	P
	description	binding site for residue OLC B 602
	source	: AF2

92)	chain	A
	residue	89
	type
	sequence	V
	description	binding site for residue OLC B 602
	source	: AF2

93)	chain	A
	residue	92
	type
	sequence	F
	description	binding site for residue OLC B 602
	source	: AF2

94)	chain	B
	residue	178
	type
	sequence	M
	description	binding site for residue OLC B 602
	source	: AF2

95)	chain	B
	residue	494
	type
	sequence	L
	description	binding site for residue OLC B 602
	source	: AF2

96)	chain	B
	residue	498
	type
	sequence	F
	description	binding site for residue OLC B 602
	source	: AF2

97)	chain	B
	residue	7
	type
	sequence	I
	description	binding site for residue OLC B 603
	source	: AF3

98)	chain	B
	residue	13
	type
	sequence	R
	description	binding site for residue OLC B 603
	source	: AF3

99)	chain	B
	residue	46
	type
	sequence	A
	description	binding site for residue OLC B 603
	source	: AF3

100)	chain	B
	residue	47
	type
	sequence	L
	description	binding site for residue OLC B 603
	source	: AF3

101)	chain	B
	residue	49
	type
	sequence	F
	description	binding site for residue OLC B 603
	source	: AF3

102)	chain	B
	residue	134
	type
	sequence	V
	description	binding site for residue OLC B 604
	source	: AF4

103)	chain	B
	residue	394
	type
	sequence	E
	description	binding site for residue OLC B 604
	source	: AF4

104)	chain	B
	residue	488
	type
	sequence	N
	description	binding site for residue OLC B 604
	source	: AF4

105)	chain	B
	residue	489
	type
	sequence	W
	description	binding site for residue OLC B 604
	source	: AF4

106)	chain	B
	residue	492
	type
	sequence	W
	description	binding site for residue OLC B 604
	source	: AF4

107)	chain	B
	residue	499
	type
	sequence	G
	description	binding site for residue OLC B 604
	source	: AF4

108)	chain	B
	residue	54
	type
	sequence	L
	description	binding site for residue OLC B 605
	source	: AF5

109)	chain	B
	residue	96
	type
	sequence	L
	description	binding site for residue OLC B 605
	source	: AF5

110)	chain	B
	residue	103
	type
	sequence	L
	description	binding site for residue OLC B 605
	source	: AF5

111)	chain	B
	residue	210
	type
	sequence	Y
	description	binding site for residue OLC B 606
	source	: AF6

112)	chain	B
	residue	211
	type
	sequence	I
	description	binding site for residue OLC B 606
	source	: AF6

113)	chain	B
	residue	212
	type
	sequence	Q
	description	binding site for residue OLC B 606
	source	: AF6

114)	chain	B
	residue	209
	type
	sequence	R
	description	binding site for residue OLC B 607
	source	: AF7

115)	chain	B
	residue	137
	type
	sequence	F
	description	binding site for residue OLC B 608
	source	: AF8

116)	chain	B
	residue	141
	type
	sequence	W
	description	binding site for residue OLC B 608
	source	: AF8

117)	chain	B
	residue	488
	type
	sequence	N
	description	binding site for residue OLC B 608
	source	: AF8

118)	chain	B
	residue	492
	type
	sequence	W
	description	binding site for residue OLC B 608
	source	: AF8

119)	chain	B
	residue	141
	type
	sequence	W
	description	binding site for residue GOL B 609
	source	: AF9

120)	chain	B
	residue	143
	type
	sequence	L
	description	binding site for residue GOL B 609
	source	: AF9

121)	chain	B
	residue	144
	type
	sequence	T
	description	binding site for residue GOL B 609
	source	: AF9

122)	chain	A
	residue	239
	type
	sequence	E
	description	binding site for residue GOL B 610
	source	: AG1

123)	chain	A
	residue	277
	type
	sequence	Q
	description	binding site for residue GOL B 610
	source	: AG1

124)	chain	B
	residue	277
	type
	sequence	Q
	description	binding site for residue GOL B 610
	source	: AG1

125)	chain	B
	residue	280
	type
	sequence	F
	description	binding site for residue GOL B 610
	source	: AG1

126)	chain	B
	residue	32
	type
	sequence	D
	description	binding site for residue GOL B 611
	source	: AG2

127)	chain	A
	residue	247
	type
	sequence	K
	description	binding site for residue GOL B 612
	source	: AG3

128)	chain	A
	residue	251
	type
	sequence	N
	description	binding site for residue GOL B 612
	source	: AG3

129)	chain	B
	residue	244
	type
	sequence	N
	description	binding site for residue GOL B 612
	source	: AG3

130)	chain	A
	residue	49-52
	type	TOPO_DOM
	sequence	FNRR
	description	Cytoplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI1

131)	chain	A
	residue	117-120
	type	TOPO_DOM
	sequence	PKTT
	description	Cytoplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI1

132)	chain	A
	residue	190-191
	type	TOPO_DOM
	sequence	RN
	description	Cytoplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI1

133)	chain	B
	residue	49-52
	type	TOPO_DOM
	sequence	FNRR
	description	Cytoplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI1

134)	chain	B
	residue	117-120
	type	TOPO_DOM
	sequence	PKTT
	description	Cytoplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI1

135)	chain	B
	residue	190-191
	type	TOPO_DOM
	sequence	RN
	description	Cytoplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI1

136)	chain	A
	residue	10-27
	type	TRANSMEM
	sequence	QRIRLLLALLFGACGTLA
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

137)	chain	B
	residue	34-48
	type	TRANSMEM
	sequence	WPAAIISLMGLQALT
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

138)	chain	B
	residue	53-68
	type	TRANSMEM
	sequence	PLQSAAIGFCWGFGLF
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

139)	chain	B
	residue	87-116
	type	TRANSMEM
	sequence	GPVNIFLVVLLAAYLSLYTGLFAGVLSRLW
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

140)	chain	B
	residue	121-141
	type	TRANSMEM
	sequence	WLRVAIAAPALWQVTEFLRGW
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

141)	chain	B
	residue	169-189
	type	TRANSMEM
	sequence	VEAINFLLMMVSGLLALALVK
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

142)	chain	B
	residue	192-210
	type	TRANSMEM
	sequence	WRPLVVAVVLFALPFPLRY
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

143)	chain	B
	residue	488-508
	type	TRANSMEM
	sequence	NWPLWVLTALFGFAAVLMSLR
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

144)	chain	A
	residue	34-48
	type	TRANSMEM
	sequence	WPAAIISLMGLQALT
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

145)	chain	A
	residue	53-68
	type	TRANSMEM
	sequence	PLQSAAIGFCWGFGLF
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

146)	chain	A
	residue	87-116
	type	TRANSMEM
	sequence	GPVNIFLVVLLAAYLSLYTGLFAGVLSRLW
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

147)	chain	A
	residue	121-141
	type	TRANSMEM
	sequence	WLRVAIAAPALWQVTEFLRGW
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

148)	chain	A
	residue	169-189
	type	TRANSMEM
	sequence	VEAINFLLMMVSGLLALALVK
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

149)	chain	A
	residue	192-210
	type	TRANSMEM
	sequence	WRPLVVAVVLFALPFPLRY
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

150)	chain	A
	residue	488-508
	type	TRANSMEM
	sequence	NWPLWVLTALFGFAAVLMSLR
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

151)	chain	B
	residue	10-27
	type	TRANSMEM
	sequence	QRIRLLLALLFGACGTLA
	description	Helical => ECO:0000269\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI2

152)	chain	A
	residue	28-33
	type	TOPO_DOM
	sequence	FSPYDV
	description	Periplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI3

153)	chain	A
	residue	69-86
	type	TOPO_DOM
	sequence	GSGINWVYVSIATFGGMP
	description	Periplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI3

154)	chain	A
	residue	142-168
	type	TOPO_DOM
	sequence	VLTGFPWLQFGYSQIDGPLKGLAPIMG
	description	Periplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI3

155)	chain	A
	residue	211-487
	type	TOPO_DOM
	sequence	IQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYY NATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRD KGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPYSYESA DRYNKNHLVPFGEFVPLESILRPLAPFFDLPMSSFSRGPY IQPPLSANGIELTAAIAYEIILGEQVRDNFRPDTDYLLTI SNDAWFGKSIGPWQHFQMARMRALELARPLLRSTNNGITA VIGPQGEIQAMIPQFTREVLTTNVTPTTGLTPYARTG
	description	Periplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI3

156)	chain	B
	residue	28-33
	type	TOPO_DOM
	sequence	FSPYDV
	description	Periplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI3

157)	chain	B
	residue	69-86
	type	TOPO_DOM
	sequence	GSGINWVYVSIATFGGMP
	description	Periplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI3

158)	chain	B
	residue	142-168
	type	TOPO_DOM
	sequence	VLTGFPWLQFGYSQIDGPLKGLAPIMG
	description	Periplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI3

159)	chain	B
	residue	211-487
	type	TOPO_DOM
	sequence	IQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYY NATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRD KGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPYSYESA DRYNKNHLVPFGEFVPLESFSRGPYIQPPLSANGIELTAA IAYEIILGEQVRDNFRPDTDYLLTISNDAWFGKSIGPWQH FQMARMRALELARPLLRSTNNGITAVIGPQGEIQAMIPQF TREVLTTNVTPTTGLTPYARTG
	description	Periplasmic => ECO:0000269\|PubMed:28675161, ECO:0000269\|PubMed:28885614
	source	Swiss-Prot : SWS_FT_FI3

160)	chain	A
	residue	267
	type	ACT_SITE
	sequence	E
	description	Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_01148, ECO:0000305\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI4

161)	chain	B
	residue	267
	type	ACT_SITE
	sequence	E
	description	Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_01148, ECO:0000305\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI4

162)	chain	A
	residue	335
	type	ACT_SITE
	sequence	K
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_01148, ECO:0000305\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI5

163)	chain	B
	residue	335
	type	ACT_SITE
	sequence	K
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_01148, ECO:0000305\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI5

164)	chain	A
	residue	387
	type	ACT_SITE
	sequence	A
	description	Nucleophile => ECO:0000255\|HAMAP-Rule:MF_01148, ECO:0000305\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI6

165)	chain	B
	residue	387
	type	ACT_SITE
	sequence	A
	description	Nucleophile => ECO:0000255\|HAMAP-Rule:MF_01148, ECO:0000305\|PubMed:28675161
	source	Swiss-Prot : SWS_FT_FI6