ID A0A1C7D309_9FABA Unreviewed; 81 AA. AC A0A1C7D309; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 30-NOV-2016, entry version 2. DE RecName: Full=ATP synthase subunit c, chloroplastic {ECO:0000256|RuleBase:RU004221}; GN Name=atpH {ECO:0000313|EMBL:AHY33062.1}; OS Indigofera tinctoria. OG Plastid; Chloroplast {ECO:0000313|EMBL:AHY33062.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC 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., RA 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 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|RuleBase:RU004221}. 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. {ECO:0000256|RuleBase:RU004221}. 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 four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha CC and beta chains form an alternating ring which encloses part of CC the gamma chain. F(1) is attached to F(0) by a central stalk CC formed by the gamma and epsilon chains, while a peripheral stalk CC is formed by the delta, b and b' chains. CC {ECO:0000256|RuleBase:RU004221}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|RuleBase:RU004221}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU004221}. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC {ECO:0000256|RuleBase:RU004221}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {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 GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR Gene3D; 1.20.20.10; -; 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; IPR002379; ATPase_proteolipid_c-like_dom. 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|RuleBase:RU004221}; KW CF(0) {ECO:0000256|RuleBase:RU004221}; KW Chloroplast {ECO:0000256|RuleBase:RU004221, KW ECO:0000313|EMBL:AHY33062.1}; KW Hydrogen ion transport {ECO:0000256|RuleBase:RU004221}; KW Ion transport {ECO:0000256|RuleBase:RU004221}; KW Lipid-binding {ECO:0000256|RuleBase:RU004221}; KW Membrane {ECO:0000256|RuleBase:RU004221}; KW Plastid {ECO:0000313|EMBL:AHY33062.1}; KW Thylakoid {ECO:0000256|RuleBase:RU004221}; KW Transmembrane {ECO:0000256|RuleBase:RU004221}; KW Transmembrane helix {ECO:0000256|RuleBase:RU004221}; KW Transport {ECO:0000256|RuleBase:RU004221}. FT TRANSMEM 57 77 Helical. {ECO:0000256|RuleBase:RU004221}. SQ SEQUENCE 81 AA; 7990 MW; D418DBC23EE09FA1 CRC64; MNPLISAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM EALTIYGLVV ALALLFANPF V //