ID A0A1C7D309_9FABA Unreviewed; 81 AA. AC A0A1C7D309; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 29-SEP-2021, entry version 19. DE RecName: Full=ATP synthase subunit c, chloroplastic {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=ATPase subunit III {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=atpH {ECO:0000256|HAMAP-Rule:MF_01396, GN ECO:0000313|EMBL:AHY33062.1}; OS Indigofera tinctoria. OG Plastid; Chloroplast {ECO:0000313|EMBL:AHY33062.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Indigofereae; Indigofera. OX NCBI_TaxID=198914 {ECO:0000313|EMBL:AHY33062.1}; RN [1] {ECO:0000313|EMBL:AHY33062.1} RP NUCLEOTIDE SEQUENCE. RA Sabir J., Schwarz E.N., Baeshen N.A., Mutwakil M., Jansen R.K., Ruhlman T.; RT "Comparative Genomics of legumes."; RL Submitted (FEB-2014) 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, ECO:0000256|RuleBase:RU004221}. 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 -!- FUNCTION: This protein is one of the chains of the nonenzymatic CC membrane component (F0) of mitochondrial ATPase. CC {ECO:0000256|ARBA:ARBA00002351}. 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:0000256|HAMAP-Rule:MF_01396, CC ECO:0000256|RuleBase:RU004221}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01396, CC ECO:0000256|RuleBase:RU004221}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01396, ECO:0000256|RuleBase:RU004221}. CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as CC CF(1)CF(0). {ECO:0000256|HAMAP-Rule:MF_01396}. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC {ECO:0000256|ARBA:ARBA00006704, ECO:0000256|HAMAP-Rule:MF_01396, CC ECO:0000256|RuleBase:RU004221}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01396, CC ECO:0000256|RuleBase:RU004221}. 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; KJ468098; AHY33062.1; -; Genomic_DNA. DR SMR; A0A1C7D309; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01396}; KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01396}; KW Chloroplast {ECO:0000256|RuleBase:RU004221, ECO:0000313|EMBL:AHY33062.1}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01396}; 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 Plastid {ECO:0000313|EMBL:AHY33062.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01396, ECO:0000256|RuleBase:RU004221}; 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 57..77 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396, FT ECO:0000256|RuleBase:RU004221" FT DOMAIN 11..73 FT /note="ATP-synt_C" FT /evidence="ECO:0000259|Pfam:PF00137" FT SITE 61 FT /note="Reversibly protonated during proton transport" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01396" SQ SEQUENCE 81 AA; 7990 MW; D418DBC23EE09FA1 CRC64; MNPLISAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM EALTIYGLVV ALALLFANPF V //