ID A0A372V7G5_9FIRM Unreviewed; 87 AA. AC A0A372V7G5; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 07-APR-2021, entry version 13. 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 ECO:0000313|EMBL:RGC99690.1}; GN ORFNames=DW194_05430 {ECO:0000313|EMBL:RGC99690.1}; OS Subdoligranulum sp. AM16-9. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Subdoligranulum; unclassified Subdoligranulum. OX NCBI_TaxID=2302960 {ECO:0000313|EMBL:RGC99690.1, ECO:0000313|Proteomes:UP000262449}; RN [1] {ECO:0000313|EMBL:RGC99690.1, ECO:0000313|Proteomes:UP000262449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM16-9 {ECO:0000313|EMBL:RGC99690.1, RC ECO:0000313|Proteomes:UP000262449}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) 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:0000256|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:0000256|HAMAP-Rule:MF_01396}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01396}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC {ECO:0000256|ARBA:ARBA00006704, ECO:0000256|HAMAP-Rule:MF_01396}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01396}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RGC99690.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QVGL01000005; RGC99690.1; -; Genomic_DNA. DR RefSeq; WP_009324702.1; NZ_QVGL01000005.1. DR EnsemblBacteria; RGC99690; RGC99690; DW194_05430. DR GeneID; 60380055; -. DR Proteomes; UP000262449; Unassembled WGS sequence. 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:0016787; F:hydrolase activity; 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 {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01396}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396}; KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01396}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01396}; Hydrolase {ECO:0000313|EMBL:RGC99690.1}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01396}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121, ECO:0000256|HAMAP- KW Rule:MF_01396}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01396}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01396}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01396}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01396}. FT TRANSMEM 66..86 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396" FT DOMAIN 14..75 FT /note="ATP-synt_C" FT /evidence="ECO:0000259|Pfam:PF00137" FT SITE 62 FT /note="Reversibly protonated during proton transport" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396" SQ SEQUENCE 87 AA; 8600 MW; 62D3C223A40F886B CRC64; MLEKAIILAG CAVGAGLALI AGIGPGIGEG YAVGKACEAI GRQPECKGDV TSTMLLGCAI AETTGIYGFV TGLLLIFVAP GIFMGLL //