(data stored in SCRATCH zone)

SWISSPROT: C6B2N8_RHILS

ID   C6B2N8_RHILS            Unreviewed;       250 AA.
AC   C6B2N8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=ATP synthase subunit a {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000256|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000256|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000256|HAMAP-Rule:MF_01393};
GN   OrderedLocusNames=Rleg_0554 {ECO:0000313|EMBL:ACS54858.1};
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:ACS54858.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54858.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54858.1,
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: Key component of the proton channel; it plays a direct
CC       role in the translocation of protons across the membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a(1), b(2) and c(9-12). The alpha and
CC       beta chains form an alternating ring which encloses part of the
CC       gamma chain. CF(1) is attached to CF(0) by a central stalk formed
CC       by the gamma and epsilon chains, while a peripheral stalk is
CC       formed by the delta and b chains. {ECO:0000256|HAMAP-
CC       Rule:MF_01393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01393}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01393}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU000483}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU000483}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01393, ECO:0000256|RuleBase:RU000483}.
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DR   EMBL; CP001622; ACS54858.1; -; Genomic_DNA.
DR   RefSeq; WP_012756240.1; NC_012850.1.
DR   ProteinModelPortal; C6B2N8; -.
DR   EnsemblBacteria; ACS54858; ACS54858; Rleg_0554.
DR   KEGG; rlg:Rleg_0554; -.
DR   HOGENOM; HOG000253874; -.
DR   KO; K02108; -.
DR   OMA; GMFPYFF; -.
DR   OrthoDB; POG091H02LL; -.
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   Gene3D; 1.20.120.220; -; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B2N8.
DR   SWISS-2DPAGE; C6B2N8.
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01393};
KW   CF(0) {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01393};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01393,
KW   ECO:0000256|RuleBase:RU000483}.
FT   TRANSMEM     29     47       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM     84    108       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    114    134       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    141    165       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    185    214       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
FT   TRANSMEM    221    242       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01393}.
SQ   SEQUENCE   250 AA;  26886 MW;  37BCFB194CDDBA8D CRC64;
     MSNDPTHQFL IQKIVPIEIG GIDFSFTNAS LFMAVSAAAA AGFLYFATSN RAIVPGRSQS
     VAEMSYEFIA NMLKEGAGKQ GMKFFPLVFS LFMFVLTANL LGMFPYFFTV TSQIIVTFAL
     AILVIGTVLV YGFYKHGFHF LNVFVPSGVP GLLLPLVVTI EIISFLSRPI SLSVRLFANM
     LAGHITLKVF AGFVASLGTM GALGIGGAVL PLIMTVALTG LEFLVAFLQA YVFAVLTCMY
     LNDAIHPGGH
//

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