(data stored in ACNUC7421 zone)


ID   C6B2N9_RHILS            Unreviewed;        75 AA.
AC   C6B2N9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 54.
DE   RecName: Full=ATP synthase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE   AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE   AltName: Full=F-type ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE            Short=F-ATPase subunit c {ECO:0000256|HAMAP-Rule:MF_01396};
DE   AltName: Full=Lipid-binding protein {ECO:0000256|HAMAP-Rule:MF_01396};
GN   Name=atpE {ECO:0000256|HAMAP-Rule:MF_01396};
GN   OrderedLocusNames=Rleg_0555 {ECO:0000313|EMBL:ACS54859.1};
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:ACS54859.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54859.1, ECO:0000313|Proteomes:UP000002256}
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54859.1,
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: 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_01396}.
CC   -!- FUNCTION: Key component of the F(0) channel; it plays a direct
CC       role in translocation across the membrane. A homomeric c-ring of
CC       between 10-14 subunits forms the central stalk rotor element with
CC       the F(1) delta and epsilon subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_01396}.
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_01396}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01396}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01396}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01396}.
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DR   EMBL; CP001622; ACS54859.1; -; Genomic_DNA.
DR   RefSeq; WP_003545854.1; NC_012850.1.
DR   ProteinModelPortal; C6B2N9; -.
DR   EnsemblBacteria; ACS54859; ACS54859; Rleg_0555.
DR   GeneID; 23434718; -.
DR   KEGG; rlg:Rleg_0555; -.
DR   HOGENOM; HOG000235245; -.
DR   KO; K02110; -.
DR   OrthoDB; POG091H043Z; -.
DR   BioCyc; RLEG395491:GHX2-555-MONOMER; -.
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:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP.
DR   Gene3D;; -; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   PANTHER; PTHR10031; PTHR10031; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   SUPFAM; SSF81333; SSF81333; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW   CF(0) {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Lipid-binding {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01396}.
FT   TRANSMEM      6     29       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01396}.
FT   TRANSMEM     50     74       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01396}.
FT   DOMAIN        9     71       ATP-synt_C. {ECO:0000259|Pfam:PF00137}.
FT   SITE         58     58       Reversibly protonated during proton
FT                                transport. {ECO:0000256|HAMAP-Rule:
FT                                MF_01396}.
SQ   SEQUENCE   75 AA;  7604 MW;  FAD144CB3C6E1642 CRC64;

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