(data stored in SCRATCH zone)

SWISSPROT: C6B2P1_RHILS

ID   C6B2P1_RHILS            Unreviewed;       163 AA.
AC   C6B2P1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
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   OrderedLocusNames=Rleg_0557 {ECO:0000313|EMBL:ACS54861.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54861.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54861.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54861.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). {ECO:0000256|HAMAP-
CC       Rule:MF_01398}.
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
CC       presence of a proton or sodium gradient. F-type ATPases consist of
CC       two structural domains, F(1) containing the extramembraneous
CC       catalytic core and F(0) containing the membrane proton channel,
CC       linked together by a central stalk and a peripheral stalk. During
CC       catalysis, ATP synthesis in the catalytic domain of F(1) is
CC       coupled via a rotary mechanism of the central stalk subunits to
CC       proton translocation. {ECO:0000256|HAMAP-Rule:MF_01398}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
CC       core - and F(0) - the membrane proton channel. F(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
CC       has three main subunits: a(1), b(2) and c(10-14). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. F(1) is attached to F(0) by a central stalk formed by
CC       the gamma and epsilon chains, while a peripheral stalk is formed
CC       by the delta and b chains. {ECO:0000256|HAMAP-Rule:MF_01398}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01398}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01398}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01398, ECO:0000256|RuleBase:RU003848}.
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DR   EMBL; CP001622; ACS54861.1; -; Genomic_DNA.
DR   RefSeq; WP_012756242.1; NC_012850.1.
DR   EnsemblBacteria; ACS54861; ACS54861; Rleg_0557.
DR   KEGG; rlg:Rleg_0557; -.
DR   HOGENOM; HOG000251920; -.
DR   KO; K02109; -.
DR   OMA; KVPGMMA; -.
DR   OrthoDB; POG091H029A; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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-HAMAP.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   Pfam; PF00430; ATP-synt_B; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B2P1.
DR   SWISS-2DPAGE; C6B2P1.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01398};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01398};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01398};
KW   CF(0) {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01398};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01398};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01398,
KW   ECO:0000256|RuleBase:RU003848}.
FT   TRANSMEM      6     25       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01398}.
FT   COILED       32     98       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   163 AA;  18082 MW;  9B5895ACBDCB97DF CRC64;
     MEFAFDATFF AFVGLVLFLA LVVYLKVPGM MARSLDDRAD QIRNELAEAK RLREEAQHLL
     AEYQRKRKEA EAEAAHIVAA AEREAEMLTA EAKKKTEEFV ANRTALSEQK IKQAEVEAMK
     AVRSAAVDLA IAAAETVLAK RADTKIQSEL FGNAVGQVKT RLN
//

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