(data stored in SCRATCH zone)

SWISSPROT: Q13IW7_PARXL

ID   Q13IW7_PARXL            Unreviewed;        82 AA.
AC   Q13IW7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 99.
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   ORFNames=Bxe_C0045 {ECO:0000313|EMBL:ABE35972.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE35972.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE35972.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE35972.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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       ECO:0000256|SAAS:SAAS01082772}.
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; CP000272; ABE35972.1; -; Genomic_DNA.
DR   RefSeq; WP_011493232.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0045; -.
DR   EnsemblBacteria; ABE35972; ABE35972; Bxe_C0045.
DR   GeneID; 4009833; -.
DR   KEGG; bxb:DR64_8380; -.
DR   KEGG; bxe:Bxe_C0045; -.
DR   PATRIC; fig|266265.5.peg.7824; -.
DR   eggNOG; ENOG4105VH4; Bacteria.
DR   eggNOG; COG0636; LUCA.
DR   HOGENOM; HOG000235245; -.
DR   KO; K02110; -.
DR   OMA; ESIAIYC; -.
DR   OrthoDB; 2078221at2; -.
DR   BioCyc; BXEN266265:BXE_RS36975-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
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-UniRule.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.20.10; -; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR   InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   PANTHER; PTHR10031; PTHR10031; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; SSF81333; 1.
DR   TIGRFAMs; TIGR01260; ATP_synt_c; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13IW7.
DR   SWISS-2DPAGE; Q13IW7.
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   ECO:0000256|SAAS:SAAS01082763};
KW   CF(0) {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396};
KW   Hydrolase {ECO:0000313|EMBL:ABE35972.1};
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:UP000001817};
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     51     77       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01396}.
FT   DOMAIN       11     73       ATP-synt_C. {ECO:0000259|Pfam:PF00137}.
FT   SITE         61     61       Reversibly protonated during proton
FT                                transport. {ECO:0000256|HAMAP-Rule:
FT                                MF_01396}.
SQ   SEQUENCE   82 AA;  8420 MW;  E42D664F77A11B2B CRC64;
     MTNLIQVISI LAAAIAVSFG AIGPALGEGR AVAAAMDALA RQPESAGTIS RTLFVGLAMI
     ETMAIYCLVI ALLVLFANPF VK
//

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