ID A0A231NZ13_9DELT Unreviewed; 473 AA. AC A0A231NZ13; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 25-APR-2018, entry version 5. DE RecName: Full=ATP synthase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347}; DE EC=3.6.3.14 {ECO:0000256|HAMAP-Rule:MF_01347}; DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347}; DE AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347}; GN Name=atpD {ECO:0000256|HAMAP-Rule:MF_01347}; GN ORFNames=BCS36_11675 {ECO:0000313|EMBL:OXS27698.1}; OS Desulfovibrio sp. MES5. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=1899016 {ECO:0000313|EMBL:OXS27698.1}; RN [1] {ECO:0000313|EMBL:OXS27698.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MES5 {ECO:0000313|EMBL:OXS27698.1}; RA Marshall C., Ross D.E., Handley K., Weisenhorn P., Edirisinghe J., RA Henry C., Gilbert J., May H., Norman R.S.; RT "Metabolic Reconstruction and Modeling Microbial Electrosynthesis."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The catalytic sites are hosted CC primarily by the beta subunits. {ECO:0000256|HAMAP-Rule:MF_01347}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {ECO:0000256|HAMAP-Rule:MF_01347}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01347}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|HAMAP-Rule:MF_01347}. 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:OXS27698.1}. 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; MJUZ01000052; OXS27698.1; -; Genomic_DNA. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.1140.10; -; 1. DR HAMAP; MF_01347; ATP_synth_beta_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR005722; ATP_synth_F1_bsu. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N. DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR024034; ATPase_F1/V1_b/a_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01347}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01347}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347}; KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01347}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01347}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01347}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01347}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01347}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01347}. FT DOMAIN 148 334 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 156 163 ATP. {ECO:0000256|HAMAP-Rule:MF_01347}. SQ SEQUENCE 473 AA; 51412 MW; 1A715460A8A9A071 CRC64; MSKNIGKIVQ VIGAVVDVEF TDGNLPNIFT ALEIKNPNNT DAPYLVCEVA QHLGDNVVRT IAMDATEGLV RGMEAVDTGQ PIMVPVGKPS VGRILNVIGH PVDELGPINA EKYYPIHRPA PAFTDQNTKV ELLETGIKVV DLLVPFPKGG KMGLFGGAGV GKTVILMEMI NNIAKQHGGS SVFAGVGERT REGNDLYHEL KDAGVLERAT LVYGQMNEPP GARARVALTA LACAEYFRDE EHQDVLLFID NIFRFTQAGS EVSALLGRMP SAVGYQPTLG TDLGSLQERI TSTNTGSITS VQAVYVPADD LTDPAPATTF SHLDGTLVLS RQIAELGIYP AVDPLDSTSR ILAPDVVGDD HYMVARRVQM VLQKYKELQD IIAILGMDEL SDEDKLTVAR ARRIQRFLSQ PFHVAETFTG TPGQYVKLED TIKGFKGILD GAYDHMAEGD FYMLGGIEQA VAKYEQRKLQ EEN //