eF-site ID 4cbj-CDEFGH
PDB Code 4cbj
Chain C, D, E, F, G, H

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Title The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology
Classification TRANSFERASE
Compound ATP SYNTHASE SUBUNIT C
Source ORGANISM_SCIENTIFIC: BACILLUS PSEUDOFIRMUS OF4;
Sequence C:  MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRG
TLQTLMFIGVALAEAVPIIAIVISLLILF
D:  MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRG
TLQTLMFIGVALAEAVPIIAIVISLLILF
E:  MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRG
TLQTLMFIGVALAEAVPIIAIVISLLILF
F:  MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRG
TLQTLMFIGVALAEAVPIIAIVISLLILF
G:  MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRG
TLQTLMFIGVALAEAVPIIAIVISLLILF
H:  MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRG
TLQTLMFIGVALAEAVPIIAIVISLLILF
Description


Functional site

1) chain C
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV B 200
source : AC3

2) chain C
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV C 200
source : AC4

3) chain C
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE DPV C 200
source : AC4

4) chain D
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV C 200
source : AC4

5) chain D
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE DPV C 200
source : AC4

6) chain C
residue 23
type
sequence I
description BINDING SITE FOR RESIDUE DPV D 200
source : AC5

7) chain C
residue 35
type
sequence Q
description BINDING SITE FOR RESIDUE TAM D 1070
source : AC6

8) chain D
residue 34
type
sequence R
description BINDING SITE FOR RESIDUE TAM D 1070
source : AC6

9) chain D
residue 35
type
sequence Q
description BINDING SITE FOR RESIDUE TAM D 1070
source : AC6

10) chain D
residue 23
type
sequence I
description BINDING SITE FOR RESIDUE DPV E 200
source : AC7

11) chain E
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV E 200
source : AC7

12) chain F
residue 19
type
sequence I
description BINDING SITE FOR RESIDUE DPV F 200
source : AC8

13) chain F
residue 23
type
sequence I
description BINDING SITE FOR RESIDUE DPV F 200
source : AC8

14) chain F
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV F 200
source : AC8

15) chain F
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE DPV F 200
source : AC8

16) chain G
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV F 200
source : AC8

17) chain F
residue 23
type
sequence I
description BINDING SITE FOR RESIDUE DPV G 200
source : AC9

18) chain G
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV G 200
source : AC9

19) chain G
residue 30
type
sequence E
description BINDING SITE FOR RESIDUE DPV G 200
source : AC9

20) chain H
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV G 200
source : AC9

21) chain H
residue 26
type
sequence K
description BINDING SITE FOR RESIDUE DPV H 200
source : BC1

22) chain C
residue 33-54
type prosite
sequence TRQPELRGTLQTLMFIGVALAE
description ATPASE_C ATP synthase c subunit signature. TRQPelrgtLqTlmFIgvaLaE
source prosite : PS00605

23) chain C
residue 5-25
type TRANSMEM
sequence GAAIAAGLAAVAGAIAVAIIV
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

24) chain G
residue 47-67
type TRANSMEM
sequence FIGVALAEAVPIIAIVISLLI
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

25) chain H
residue 5-25
type TRANSMEM
sequence GAAIAAGLAAVAGAIAVAIIV
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

26) chain H
residue 47-67
type TRANSMEM
sequence FIGVALAEAVPIIAIVISLLI
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

27) chain C
residue 47-67
type TRANSMEM
sequence FIGVALAEAVPIIAIVISLLI
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

28) chain D
residue 5-25
type TRANSMEM
sequence GAAIAAGLAAVAGAIAVAIIV
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

29) chain D
residue 47-67
type TRANSMEM
sequence FIGVALAEAVPIIAIVISLLI
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

30) chain E
residue 5-25
type TRANSMEM
sequence GAAIAAGLAAVAGAIAVAIIV
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

31) chain E
residue 47-67
type TRANSMEM
sequence FIGVALAEAVPIIAIVISLLI
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

32) chain F
residue 5-25
type TRANSMEM
sequence GAAIAAGLAAVAGAIAVAIIV
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

33) chain F
residue 47-67
type TRANSMEM
sequence FIGVALAEAVPIIAIVISLLI
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

34) chain G
residue 5-25
type TRANSMEM
sequence GAAIAAGLAAVAGAIAVAIIV
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

35) chain C
residue 54
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

36) chain D
residue 54
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

37) chain E
residue 54
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

38) chain F
residue 54
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

39) chain G
residue 54
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

40) chain H
residue 54
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2


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