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}.
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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
//