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ATPL2_CERS1
ID   ATPL2_CERS1             Reviewed;          83 AA.
AC   A3PS63;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=ATP synthase subunit c 2 {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=ATP synthase F(0) sector subunit c 2 {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=F-type ATPase subunit c 2 {ECO:0000255|HAMAP-Rule:MF_01396};
DE            Short=F-ATPase subunit c 2 {ECO:0000255|HAMAP-Rule:MF_01396};
DE   AltName: Full=Lipid-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_01396};
GN   Name=atpE2 {ECO:0000255|HAMAP-Rule:MF_01396};
GN   OrderedLocusNames=Rsph17029_4101;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OG   Plasmid pRSPH01.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of plasmid pRSPH01 of Rhodobacter sphaeroides ATCC
RT   17029.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-
CC       Rule:MF_01396}.
CC   -!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
CC       translocation across the membrane. A homomeric c-ring of between 10-14
CC       subunits forms the central stalk rotor element with the F(1) delta and
CC       epsilon subunits. {ECO:0000255|HAMAP-Rule:MF_01396}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC       subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC       form an alternating ring which encloses part of the gamma chain. F(1)
CC       is attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta, b and b'
CC       chains. {ECO:0000255|HAMAP-Rule:MF_01396}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01396}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01396}.
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DR   EMBL; CP000579; ABN79179.1; -; Genomic_DNA.
DR   RefSeq; WP_002724764.1; NC_009040.1.
DR   AlphaFoldDB; A3PS63; -.
DR   SMR; A3PS63; -.
DR   EnsemblBacteria; ABN79179; ABN79179; Rsph17029_4101.
DR   GeneID; 57472744; -.
DR   KEGG; rsh:Rsph17029_4101; -.
DR   HOGENOM; CLU_148047_2_0_5; -.
DR   OMA; ALIFRQY; -.
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   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;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Lipid-binding; Membrane; Plasmid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..83
FT                   /note="ATP synthase subunit c 2"
FT                   /id="PRO_5000227984"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT   SITE            62
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
SQ   SEQUENCE   83 AA;  8393 MW;  854E92DB7E4825E8 CRC64;
     MTPETVQIAS ILGAAFAVGI GSLGPALGEG RAVAAAMEAI ARQPEAAGTL SRTLFVGLAM
     IETMAIYCLV IALLLLFANP FTG
 
 
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