(data stored in ACNUC7421 zone)

SWISSPROT: C3MHB7_SINFN

ID   C3MHB7_SINFN            Unreviewed;       203 AA.
AC   C3MHB7;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
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=atpF2 {ECO:0000313|EMBL:ACP24245.1};
GN   Synonyms=atpF {ECO:0000256|HAMAP-Rule:MF_01398};
GN   OrderedLocusNames=NGR_c04490 {ECO:0000313|EMBL:ACP24245.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24245.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24245.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24245.1; -; Genomic_DNA.
DR   RefSeq; WP_012707030.1; NC_012587.1.
DR   RefSeq; YP_002824998.1; NC_012587.1.
DR   STRING; 394.NGR_c04490; -.
DR   EnsemblBacteria; ACP24245; ACP24245; NGR_c04490.
DR   GeneID; 7791675; -.
DR   KEGG; rhi:NGR_c04490; -.
DR   PATRIC; fig|394.7.peg.3256; -.
DR   eggNOG; ENOG4108VHN; Bacteria.
DR   eggNOG; COG0711; LUCA.
DR   HOGENOM; HOG000144126; -.
DR   KO; K02109; -.
DR   OMA; SDLDQAM; -.
DR   OrthoDB; POG091H029A; -.
DR   Proteomes; UP000001054; 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; C3MHB7.
DR   SWISS-2DPAGE; C3MHB7.
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:UP000001054};
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   Reference proteome {ECO:0000313|Proteomes:UP000001054};
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     55     74       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01398}.
FT   COILED       92    119       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   203 AA;  21236 MW;  06DF46733DE9E287 CRC64;
     MTAAYAQQST TTEGAEAHDA PAAGEVHTET GVAHEAEHGS GVFPPFDSSH FASQLLWLAI
     TFGLFYLLMS KVIIPRIGGI LEKRHDRIAQ DLDEASRLKG EADAAIASYE QELANARAKG
     HSIADTAREE AKSKATADRA AVEAELTKKI TAAETRIADI KSKALADVGA IAEETATAVV
     KQLIGGNVTK TEIAAAVKAS AGN
//

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