ID A0A372V7G5_9FIRM Unreviewed; 87 AA. AC A0A372V7G5; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 08-MAY-2019, entry version 5. 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. 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 RT 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 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|SAAS:SAAS01177937}. CC -!- SUBCELLULAR LOCATION: Cell 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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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: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; KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01396}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01396, KW ECO:0000256|SAAS:SAAS01185492}; KW CF(0) {ECO:0000256|HAMAP-Rule:MF_01396}; KW Complete proteome {ECO:0000313|Proteomes:UP000262449}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01396}; KW Hydrolase {ECO:0000313|EMBL:RGC99690.1}; 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 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 66 86 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01396}. FT DOMAIN 14 75 ATP-synt_C. {ECO:0000259|Pfam:PF00137}. FT SITE 62 62 Reversibly protonated during proton FT transport. {ECO:0000256|HAMAP-Rule: FT MF_01396}. SQ SEQUENCE 87 AA; 8600 MW; 62D3C223A40F886B CRC64; MLEKAIILAG CAVGAGLALI AGIGPGIGEG YAVGKACEAI GRQPECKGDV TSTMLLGCAI AETTGIYGFV TGLLLIFVAP GIFMGLL //