eF-site/Summary 6fms-ABCD

eF-site ID	6fms-ABCD
PDB Code	6fms
Chain	A, B, C, D

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Title	IMISX-EP of Se-LspA
Classification	HYDROLASE
Compound	Lipoprotein signal peptidase
Source	(6FMS)

Sequence	A:	PDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSXYQQIV VIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVS ASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRXVLGH VVDFILVHWQNRWYFPAFNLADSAITVGAVXLALDXF
	B:	PDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSXYQQIV VIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVS ASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRXVLGH VVDFILVHWQNRWYFPAFNLADSAITVGAVXLALDXF
	C:	PWLWITVLVFVLDQVSKAFFQAELSXYQQIVVIPDLFSWT LAYNTGAAFSFLADSSGWQRWLFALIAIVVSASLVVWLKR LKKGETWLAIALALVLGGALGNLYDRXVLGHVVDFILVHW QNRWYFPAFNLADSAITVGAVXLALDXFR
	D:	PWLWITVLVFVLDQVSKAFFQAELSXYQQIVVIPDLFSWT LAYNTGAAFSFLADSSGWQRWLFALIAIVVSASLVVWLKR LKKGETWLAIALALVLGGALGNLYDRXVLGHVVDFILVHW QNRWYFPAFNLADSAITVGAVXLALDXFR

Description

Functional site


1)	chain	A
	residue	29
	type
	sequence	F
	description	binding site for residue OLC A 201
	source	: AC1

2)	chain	A
	residue	40
	type
	sequence	I
	description	binding site for residue OLC A 201
	source	: AC1

3)	chain	A
	residue	42
	type
	sequence	V
	description	binding site for residue OLC A 202
	source	: AC2

4)	chain	A
	residue	49
	type
	sequence	W
	description	binding site for residue OLC A 202
	source	: AC2

5)	chain	A
	residue	11
	type
	sequence	P
	description	binding site for residue OLC A 203
	source	: AC3

6)	chain	A
	residue	12
	type
	sequence	W
	description	binding site for residue OLC A 203
	source	: AC3

7)	chain	A
	residue	15
	type
	sequence	I
	description	binding site for residue OLC A 203
	source	: AC3

8)	chain	D
	residue	28
	type
	sequence	A
	description	binding site for residue OLC A 203
	source	: AC3

9)	chain	D
	residue	32
	type
	sequence	A
	description	binding site for residue OLC A 203
	source	: AC3

10)	chain	A
	residue	7
	type
	sequence	F
	description	binding site for residue OLC A 204
	source	: AC4

11)	chain	A
	residue	10
	type
	sequence	L
	description	binding site for residue OLC A 204
	source	: AC4

12)	chain	A
	residue	11
	type
	sequence	P
	description	binding site for residue OLC A 204
	source	: AC4

13)	chain	A
	residue	14
	type
	sequence	W
	description	binding site for residue OLC A 204
	source	: AC4

14)	chain	D
	residue	31
	type
	sequence	Q
	description	binding site for residue OLC A 204
	source	: AC4

15)	chain	D
	residue	114
	type
	sequence	Y
	description	binding site for residue OLC A 204
	source	: AC4

16)	chain	A
	residue	70
	type
	sequence	R
	description	binding site for residue OLC A 205
	source	: AC5

17)	chain	A
	residue	117
	type
	sequence	X
	description	binding site for residue OLC A 205
	source	: AC5

18)	chain	B
	residue	8
	type
	sequence	G
	description	binding site for residue OLC B 202
	source	: AC6

19)	chain	B
	residue	9
	type
	sequence	R
	description	binding site for residue OLC B 202
	source	: AC6

20)	chain	B
	residue	11
	type
	sequence	P
	description	binding site for residue OLC B 202
	source	: AC6

21)	chain	B
	residue	12
	type
	sequence	W
	description	binding site for residue OLC B 202
	source	: AC6

22)	chain	B
	residue	15
	type
	sequence	I
	description	binding site for residue OLC B 202
	source	: AC6

23)	chain	B
	residue	93
	type
	sequence	K
	description	binding site for residue OLC B 202
	source	: AC6

24)	chain	B
	residue	104
	type
	sequence	L
	description	binding site for residue OLC B 202
	source	: AC6

25)	chain	B
	residue	10
	type
	sequence	L
	description	binding site for residue OLC B 203
	source	: AC7

26)	chain	B
	residue	14
	type
	sequence	W
	description	binding site for residue OLC B 203
	source	: AC7

27)	chain	C
	residue	114
	type
	sequence	Y
	description	binding site for residue OLC B 203
	source	: AC7

28)	chain	A
	residue	63
	type
	sequence	A
	description	binding site for residue OLC B 204
	source	: AC8

29)	chain	A
	residue	64
	type
	sequence	D
	description	binding site for residue OLC B 204
	source	: AC8

30)	chain	B
	residue	130
	type
	sequence	W
	description	binding site for residue OLC B 204
	source	: AC8

31)	chain	B
	residue	133
	type
	sequence	R
	description	binding site for residue OLC B 204
	source	: AC8

32)	chain	B
	residue	134
	type
	sequence	W
	description	binding site for residue OLC B 204
	source	: AC8

33)	chain	B
	residue	33
	type
	sequence	E
	description	binding site for residue OLC B 205
	source	: AC9

34)	chain	B
	residue	49
	type
	sequence	W
	description	binding site for residue OLC B 206
	source	: AD1

35)	chain	C
	residue	139
	type
	sequence	F
	description	binding site for residue OLC C 201
	source	: AD2

36)	chain	C
	residue	143
	type
	sequence	D
	description	binding site for residue OLC C 201
	source	: AD2

37)	chain	C
	residue	147
	type
	sequence	T
	description	binding site for residue OLC C 201
	source	: AD2

38)	chain	C
	residue	41
	type
	sequence	V
	description	binding site for residue OLC C 202
	source	: AD3

39)	chain	C
	residue	49
	type
	sequence	W
	description	binding site for residue OLC C 202
	source	: AD3

40)	chain	C
	residue	110
	type
	sequence	L
	description	binding site for residue OLC C 203
	source	: AD4

41)	chain	C
	residue	117
	type
	sequence	X
	description	binding site for residue OLC C 203
	source	: AD4

42)	chain	C
	residue	118
	type
	sequence	V
	description	binding site for residue OLC C 203
	source	: AD4

43)	chain	C
	residue	70
	type
	sequence	R
	description	binding site for residue OLC C 204
	source	: AD5

44)	chain	C
	residue	117
	type
	sequence	X
	description	binding site for residue OLC C 204
	source	: AD5

45)	chain	C
	residue	29
	type
	sequence	F
	description	binding site for residue OLC C 205
	source	: AD6

46)	chain	C
	residue	33
	type
	sequence	E
	description	binding site for residue OLC C 205
	source	: AD6

47)	chain	C
	residue	49
	type
	sequence	W
	description	binding site for residue OLC C 205
	source	: AD6

48)	chain	D
	residue	29
	type
	sequence	F
	description	binding site for residue OLC D 201
	source	: AD7

49)	chain	D
	residue	40
	type
	sequence	I
	description	binding site for residue OLC D 201
	source	: AD7

50)	chain	D
	residue	49
	type
	sequence	W
	description	binding site for residue OLC D 202
	source	: AD8

51)	chain	A
	residue	139
	type
	sequence	F
	description	binding site for residue OLC E 301
	source	: AD9

52)	chain	A
	residue	143
	type
	sequence	D
	description	binding site for residue OLC E 301
	source	: AD9

53)	chain	A
	residue	148
	type
	sequence	V
	description	binding site for residue OLC E 301
	source	: AD9

54)	chain	B
	residue	55
	type
	sequence	T
	description	binding site for residue OLC F 301
	source	: AE1

55)	chain	B
	residue	137
	type
	sequence	P
	description	binding site for residue OLC F 301
	source	: AE1

56)	chain	B
	residue	139
	type
	sequence	F
	description	binding site for residue OLC F 301
	source	: AE1

57)	chain	B
	residue	143
	type
	sequence	D
	description	binding site for residue OLC F 301
	source	: AE1

58)	chain	B
	residue	147
	type
	sequence	T
	description	binding site for residue OLC F 301
	source	: AE1

59)	chain	D
	residue	139
	type
	sequence	F
	description	binding site for residue OLC H 301
	source	: AE2

60)	chain	D
	residue	143
	type
	sequence	D
	description	binding site for residue OLC H 301
	source	: AE2

61)	chain	D
	residue	147
	type
	sequence	T
	description	binding site for residue OLC H 301
	source	: AE2

62)	chain	A
	residue	54
	type
	sequence	N
	description	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
	source	: AE3

63)	chain	A
	residue	56
	type
	sequence	G
	description	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
	source	: AE3

64)	chain	A
	residue	59
	type
	sequence	F
	description	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
	source	: AE3

65)	chain	A
	residue	73
	type
	sequence	F
	description	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
	source	: AE3

66)	chain	A
	residue	112
	type
	sequence	N
	description	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
	source	: AE3

67)	chain	A
	residue	116
	type
	sequence	R
	description	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
	source	: AE3

68)	chain	A
	residue	124
	type
	sequence	D
	description	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
	source	: AE3

69)	chain	A
	residue	143
	type
	sequence	D
	description	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203
	source	: AE3

70)	chain	B
	residue	62
	type
	sequence	L
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

71)	chain	B
	residue	73
	type
	sequence	F
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

72)	chain	B
	residue	77
	type
	sequence	A
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

73)	chain	B
	residue	80
	type
	sequence	V
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

74)	chain	B
	residue	112
	type
	sequence	N
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

75)	chain	B
	residue	116
	type
	sequence	R
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

76)	chain	B
	residue	122
	type
	sequence	V
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

77)	chain	B
	residue	124
	type
	sequence	D
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

78)	chain	B
	residue	140
	type
	sequence	N
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

79)	chain	B
	residue	143
	type
	sequence	D
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

80)	chain	B
	residue	146
	type
	sequence	I
	description	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203
	source	: AE4

81)	chain	C
	residue	54
	type
	sequence	N
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

82)	chain	C
	residue	59
	type
	sequence	F
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

83)	chain	C
	residue	73
	type
	sequence	F
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

84)	chain	C
	residue	77
	type
	sequence	A
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

85)	chain	C
	residue	112
	type
	sequence	N
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

86)	chain	C
	residue	116
	type
	sequence	R
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

87)	chain	C
	residue	122
	type
	sequence	V
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

88)	chain	C
	residue	124
	type
	sequence	D
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

89)	chain	C
	residue	143
	type
	sequence	D
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

90)	chain	C
	residue	146
	type
	sequence	I
	description	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203
	source	: AE5

91)	chain	D
	residue	54
	type
	sequence	N
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

92)	chain	D
	residue	57
	type
	sequence	A
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

93)	chain	D
	residue	59
	type
	sequence	F
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

94)	chain	D
	residue	73
	type
	sequence	F
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

95)	chain	D
	residue	80
	type
	sequence	V
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

96)	chain	D
	residue	109
	type
	sequence	A
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

97)	chain	D
	residue	112
	type
	sequence	N
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

98)	chain	D
	residue	116
	type
	sequence	R
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

99)	chain	D
	residue	124
	type
	sequence	D
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

100)	chain	D
	residue	143
	type
	sequence	D
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

101)	chain	D
	residue	146
	type
	sequence	I
	description	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203
	source	: AE6

102)	chain	A
	residue	10-30
	type	TRANSMEM
	sequence	LPWLWITVLVFVLDQVSKAFF
	description	Helical => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI1

103)	chain	B
	residue	10-30
	type	TRANSMEM
	sequence	LPWLWITVLVFVLDQVSKAFF
	description	Helical => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI1

104)	chain	A
	residue	31-67
	type	TOPO_DOM
	sequence	QAELSXYQQIVVIPDLFSWTLAYNTGAAFSFLADSSG
	description	Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI2

105)	chain	A
	residue	119-140
	type	TOPO_DOM
	sequence	LGHVVDFILVHWQNRWYFPAFN
	description	Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI2

106)	chain	B
	residue	31-67
	type	TOPO_DOM
	sequence	QAELSXYQQIVVIPDLFSWTLAYNTGAAFSFLADSSG
	description	Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI2

107)	chain	B
	residue	119-140
	type	TOPO_DOM
	sequence	LGHVVDFILVHWQNRWYFPAFN
	description	Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI2

108)	chain	C
	residue	31-67
	type	TOPO_DOM
	sequence	QAELSXYQQIVVIPDLFSWTLAYNTGAAFSFLADSSG
	description	Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI2

109)	chain	C
	residue	119-140
	type	TOPO_DOM
	sequence	LGHVVDFILVHWQNRWYFPAFN
	description	Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI2

110)	chain	D
	residue	31-67
	type	TOPO_DOM
	sequence	QAELSXYQQIVVIPDLFSWTLAYNTGAAFSFLADSSG
	description	Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI2

111)	chain	D
	residue	119-140
	type	TOPO_DOM
	sequence	LGHVVDFILVHWQNRWYFPAFN
	description	Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI2

112)	chain	A
	residue	105-117
	type	prosite
	sequence	VLGGALGNLYDRX
	description	SPASE_II Signal peptidases II signature. VlGGALGNLYDRM
	source	prosite : PS00855

113)	chain	A
	residue	68-89
	type	TRANSMEM
	sequence	WQRWLFALIAIVVSASLVVWLK
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI3

114)	chain	A
	residue	97-118
	type	TRANSMEM
	sequence	WLAIALALVLGGALGNLYDRXV
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI3

115)	chain	B
	residue	68-89
	type	TRANSMEM
	sequence	WQRWLFALIAIVVSASLVVWLK
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI3

116)	chain	B
	residue	97-118
	type	TRANSMEM
	sequence	WLAIALALVLGGALGNLYDRXV
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI3

117)	chain	C
	residue	68-89
	type	TRANSMEM
	sequence	WQRWLFALIAIVVSASLVVWLK
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI3

118)	chain	C
	residue	97-118
	type	TRANSMEM
	sequence	WLAIALALVLGGALGNLYDRXV
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI3

119)	chain	D
	residue	68-89
	type	TRANSMEM
	sequence	WQRWLFALIAIVVSASLVVWLK
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI3

120)	chain	D
	residue	97-118
	type	TRANSMEM
	sequence	WLAIALALVLGGALGNLYDRXV
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI3

121)	chain	A
	residue	90-96
	type	TOPO_DOM
	sequence	RLKKGET
	description	Cytoplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI4

122)	chain	B
	residue	90-96
	type	TOPO_DOM
	sequence	RLKKGET
	description	Cytoplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI4

123)	chain	C
	residue	90-96
	type	TOPO_DOM
	sequence	RLKKGET
	description	Cytoplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI4

124)	chain	D
	residue	90-96
	type	TOPO_DOM
	sequence	RLKKGET
	description	Cytoplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS
	source	Swiss-Prot : SWS_FT_FI4

125)	chain	A
	residue	141-154
	type	TRANSMEM
	sequence	LADSAITVGAVXLA
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0007744\|PDB:5DIR
	source	Swiss-Prot : SWS_FT_FI5

126)	chain	B
	residue	141-154
	type	TRANSMEM
	sequence	LADSAITVGAVXLA
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0007744\|PDB:5DIR
	source	Swiss-Prot : SWS_FT_FI5

127)	chain	C
	residue	141-154
	type	TRANSMEM
	sequence	LADSAITVGAVXLA
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0007744\|PDB:5DIR
	source	Swiss-Prot : SWS_FT_FI5

128)	chain	D
	residue	141-154
	type	TRANSMEM
	sequence	LADSAITVGAVXLA
	description	Helical => ECO:0000269\|PubMed:26912896, ECO:0007744\|PDB:5DIR
	source	Swiss-Prot : SWS_FT_FI5

129)	chain	A
	residue	124
	type	ACT_SITE
	sequence	D
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896
	source	Swiss-Prot : SWS_FT_FI7

130)	chain	A
	residue	143
	type	ACT_SITE
	sequence	D
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896
	source	Swiss-Prot : SWS_FT_FI7

131)	chain	B
	residue	124
	type	ACT_SITE
	sequence	D
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896
	source	Swiss-Prot : SWS_FT_FI7

132)	chain	B
	residue	143
	type	ACT_SITE
	sequence	D
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896
	source	Swiss-Prot : SWS_FT_FI7

133)	chain	C
	residue	124
	type	ACT_SITE
	sequence	D
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896
	source	Swiss-Prot : SWS_FT_FI7

134)	chain	C
	residue	143
	type	ACT_SITE
	sequence	D
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896
	source	Swiss-Prot : SWS_FT_FI7

135)	chain	D
	residue	124
	type	ACT_SITE
	sequence	D
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896
	source	Swiss-Prot : SWS_FT_FI7

136)	chain	D
	residue	143
	type	ACT_SITE
	sequence	D
	description	ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896
	source	Swiss-Prot : SWS_FT_FI7