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Database: UniProt
Entry: A0A0B2BWI4_9SPHN
LinkDB: A0A0B2BWI4_9SPHN
Original site: A0A0B2BWI4_9SPHN 
ID   A0A0B2BWI4_9SPHN        Unreviewed;       164 AA.
AC   A0A0B2BWI4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=ATP synthase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398};
DE   AltName: Full=F-type ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE            Short=F-ATPase subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
GN   Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398};
GN   ORFNames=PK98_03695 {ECO:0000313|EMBL:KHL25739.1};
OS   Croceibacterium mercuriale.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL25739.1, ECO:0000313|Proteomes:UP000030988};
RN   [1] {ECO:0000313|EMBL:KHL25739.1, ECO:0000313|Proteomes:UP000030988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coronado {ECO:0000313|EMBL:KHL25739.1,
RC   ECO:0000313|Proteomes:UP000030988};
RA   Coil D.A., Eisen J.A.;
RT   "Draft genome sequence of Kirrobacter mercurialis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged
CC       and duplicated form of b found in plants and photosynthetic bacteria.
CC       {ECO:0000256|ARBA:ARBA00025614}.
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation.
CC       {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-Rule:MF_01398}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC       subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. F(1) is
CC       attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000256|HAMAP-Rule:MF_01398}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01398}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family.
CC       {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|HAMAP-Rule:MF_01398,
CC       ECO:0000256|RuleBase:RU003848}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHL25739.1}.
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DR   EMBL; JTDN01000001; KHL25739.1; -; Genomic_DNA.
DR   RefSeq; WP_039094373.1; NZ_JTDN01000001.1.
DR   AlphaFoldDB; A0A0B2BWI4; -.
DR   STRING; 1572751.PK98_03695; -.
DR   OrthoDB; 9805716at2; -.
DR   Proteomes; UP000030988; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   PANTHER; PTHR33445:SF1; ATP SYNTHASE SUBUNIT B; 1.
DR   PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR   Pfam; PF00430; ATP-synt_B; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01398}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398};
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01398};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01398};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030988};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01398};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01398}.
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01398"
FT   COILED          103..130
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   164 AA;  18106 MW;  12AACE94F1F7BE86 CRC64;
     MPQIEQLAGT YSSQIFWLLV IFALAFFIIG LGMLPRVMDT MADRDRRIGD DLAVAQAARD
     EADTREDAWR TREAANREAA HALVNEARDQ SKRDAEQRLA SIKTSLDARL VEAEQRIDAA
     RSAAAAEIEQ VASEATQDIV ARVARIDVDA DAAHHAVRKV MVHG
//
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