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