ATPL_MOOTA
ID ATPL_MOOTA Reviewed; 74 AA.
AC Q2RFX4; O08338;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=ATP synthase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=F-type ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE Short=F-ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=Lipid-binding protein {ECO:0000255|HAMAP-Rule:MF_01396};
GN Name=atpE {ECO:0000255|HAMAP-Rule:MF_01396}; OrderedLocusNames=Moth_2383;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND OPERON STRUCTURE.
RX PubMed=9171425; DOI=10.1128/jb.179.11.3746-3755.1997;
RA Das A., Ljungdahl L.G.;
RT "Composition and primary structure of the F1F0 ATP synthase from the
RT obligately anaerobic bacterium Clostridium thermoaceticum.";
RL J. Bacteriol. 179:3746-3755(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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 three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC 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 and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01396}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01396};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; U64318; AAB51461.1; -; Genomic_DNA.
DR EMBL; CP000232; ABC20665.1; -; Genomic_DNA.
DR RefSeq; WP_011393860.1; NC_007644.1.
DR RefSeq; YP_431208.1; NC_007644.1.
DR AlphaFoldDB; Q2RFX4; -.
DR SMR; Q2RFX4; -.
DR STRING; 264732.Moth_2383; -.
DR EnsemblBacteria; ABC20665; ABC20665; Moth_2383.
DR GeneID; 61291106; -.
DR KEGG; mta:Moth_2383; -.
DR PATRIC; fig|264732.11.peg.2596; -.
DR eggNOG; COG0636; Bacteria.
DR HOGENOM; CLU_148047_2_0_9; -.
DR OMA; NIATVGY; -.
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 1: Evidence at protein level;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Lipid-binding; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..74
FT /note="ATP synthase subunit c"
FT /id="PRO_5000105889"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT SITE 57
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
SQ SEQUENCE 74 AA; 7566 MW; ADE8DF7353765F87 CRC64;
MATIGFIGVG LAIGLAALGS GLGQGIASRG ALEGMARQPE ASGDIRTTLL LALAFMEALT
LFSFVIAILM WTKL
