(data stored in ACNUC7421 zone)

SWISSPROT: C3MHB6_SINFN

ID   C3MHB6_SINFN            Unreviewed;        75 AA.
AC   C3MHB6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   30-AUG-2017, entry version 55.
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=NGR_c04480 {ECO:0000313|EMBL:ACP24244.1};
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:ACP24244.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24244.1, 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: 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01396}.
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DR   EMBL; CP001389; ACP24244.1; -; Genomic_DNA.
DR   RefSeq; WP_012707029.1; NC_012587.1.
DR   RefSeq; YP_002824997.1; NC_012587.1.
DR   STRING; 394.NGR_c04480; -.
DR   EnsemblBacteria; ACP24244; ACP24244; NGR_c04480.
DR   GeneID; 7791674; -.
DR   KEGG; rhi:NGR_c04480; -.
DR   PATRIC; fig|394.7.peg.3255; -.
DR   eggNOG; ENOG4105VD1; Bacteria.
DR   eggNOG; ENOG41121M2; LUCA.
DR   HOGENOM; HOG000235245; -.
DR   KO; K02110; -.
DR   OMA; ASFAPMM; -.
DR   OrthoDB; POG091H043Z; -.
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: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; 1.20.20.10; -; 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   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; SSF81333; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHB6.
DR   SWISS-2DPAGE; C3MHB6.
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:UP000001054};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Hydrolase {ECO:0000313|EMBL:ACP24244.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000001054};
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     48     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;  7524 MW;  481144D3B4FE1B8B CRC64;
     MEAEAAKFIG AGLACLGMAG TALGLGNIFG SYLSGALRNP SAADGQFGRL VFGFAVTEAL
     GIFSLLVALL LLFAV
//

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