ATPL_SORC5
ID ATPL_SORC5 Reviewed; 112 AA.
AC A9FGS9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=sce7980;
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56;
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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 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; AM746676; CAN98150.1; -; Genomic_DNA.
DR RefSeq; WP_012240589.1; NC_010162.1.
DR AlphaFoldDB; A9FGS9; -.
DR SMR; A9FGS9; -.
DR STRING; 448385.sce7980; -.
DR EnsemblBacteria; CAN98150; CAN98150; sce7980.
DR KEGG; scl:sce7980; -.
DR eggNOG; COG0636; Bacteria.
DR HOGENOM; CLU_148047_0_2_7; -.
DR OMA; ARPGIFI; -.
DR OrthoDB; 2063499at2; -.
DR BioCyc; SCEL448385:SCE_RS40845-MON; -.
DR Proteomes; UP000002139; 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-UniRule.
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; 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 Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 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;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..112
FT /note="ATP synthase subunit c"
FT /id="PRO_0000365923"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT SITE 93
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
SQ SEQUENCE 112 AA; 11191 MW; BF8BCCDD1C0BC113 CRC64;
MSLKSKLSLS AVVGTALVLV PAMALAQDGA ASNKYDANSW LAVAAGFAIG IAALGGTMGQ
GRAAAAALEG ISRNPGAAAR IQTPMILGLA LIESLVLLSW VIAFFLQGKI AP
