ID W8KMV5_9GAMM Unreviewed; 460 AA.
AC W8KMV5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {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=M911_16725 {ECO:0000313|EMBL:AHK80503.1};
OS Ectothiorhodospira haloalkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=421628 {ECO:0000313|EMBL:AHK80503.1, ECO:0000313|Proteomes:UP000019442};
RN [1] {ECO:0000313|EMBL:AHK80503.1, ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|EMBL:AHK80503.1,
RC ECO:0000313|Proteomes:UP000019442};
RX PubMed=25057327; DOI=10.7150/jgen.9123;
RA Singh K.S., Kirksey J., Hoff W.D., Deole R.;
RT "Draft Genome Sequence of the Extremely Halophilic Phototrophic Purple
RT Sulfur Bacterium Halorhodospira halochloris.";
RL J Genomics 2:118-120(2014).
RN [2] {ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|Proteomes:UP000019442};
RA Singh K.S.;
RT "Draft Genome Sequence of extremely halophilic bacteria Halorhodospira
RT halochloris.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The catalytic sites are hosted primarily by the
CC beta subunits. {ECO:0000256|HAMAP-Rule:MF_01347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01347};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000256|ARBA:ARBA00024342}.
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DR EMBL; CP007268; AHK80503.1; -; Genomic_DNA.
DR RefSeq; WP_025283069.1; NZ_JAJNQR010000002.1.
DR AlphaFoldDB; W8KMV5; -.
DR KEGG; hhc:M911_16725; -.
DR PATRIC; fig|1354791.3.peg.670; -.
DR HOGENOM; CLU_022398_0_2_6; -.
DR OrthoDB; 9801639at2; -.
DR Proteomes; UP000019442; Chromosome.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01347}; Reference proteome {ECO:0000313|Proteomes:UP000019442};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}.
FT DOMAIN 140..325
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 148..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ SEQUENCE 460 AA; 50059 MW; 4361E01BDB287E53 CRC64;
MSAGNIVEII GAVVDVEFPR DAVPKIYDAL MVEEVGLTLE VQQQLGDGVV RTIAMGTTDG
LRRGINVSNT GKAITVPVGK GTLGRIMDVL GKPVDNAGDV KAEDSWSIHR AAPSYEEQAG
STDLLETGIK VIDLLCPFAK GGKVGLFGGA GVGKTVNMME LIRNIAIEHS GYSVFAGVGE
RTREGNDFYH EMKDSNVLDK VALVYGQMNE PPGNRLRVAL TGLTMAEYFR DEGRDVLMFI
DNIYRYTLAG TEVSALLGRM PSAVGYQPTL AEEMGVLQER ITSTKKGSIT SIQAVYVPAD
DLTDPSPATT FAHLDATVVL SRQIAELGIY PAVDPLDSTS RQLDPLIIGQ EHYDTARAVQ
NTLQRYKELK DIIAILGMDE LSEEDKQVVS RARKIQRFLS QPFFVAEVFT GSPGKYVSLK
DTINGFQAIV DGEYDHLPEQ AFYMVGSIEE AVEKAEKLNK
//
