ATPB_VIBAL
ID ATPB_VIBAL Reviewed; 467 AA.
AC P12986;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; Synonyms=uncD;
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=138-2;
RX PubMed=2529481; DOI=10.1093/nar/17.19.7993;
RA Krumholz L.R., Esser U., Simoni R.D.;
RT "Nucleotide sequence of the unc operon of Vibrio alginolyticus.";
RL Nucleic Acids Res. 17:7993-7994(1989).
RN [2]
RP PROTEIN SEQUENCE OF 2-19.
RC STRAIN=138-2;
RX PubMed=2532151; DOI=10.1016/0014-5793(89)81657-6;
RA Dmitirev O.Y., Grinkevich V.A., Skulachev V.P.;
RT "The F1-ATPase of Vibrio alginolyticus. Purification and N-terminal
RT sequence of major subunits.";
RL FEBS Lett. 258:219-222(1989).
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:0000255|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:0000255|HAMAP-Rule:MF_01347};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; X16050; CAA34181.1; -; Genomic_DNA.
DR PIR; S06082; S06082.
DR RefSeq; WP_005383849.1; NZ_WAHT01000005.1.
DR AlphaFoldDB; P12986; -.
DR SMR; P12986; -.
DR STRING; 663.BAU10_15080; -.
DR PRIDE; P12986; -.
DR eggNOG; COG0055; Bacteria.
DR OrthoDB; 430176at2; -.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2532151"
FT CHAIN 2..467
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144486"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 467 AA; 50699 MW; 73AA2FD23B932A79 CRC64;
MATGKIVQII GAVVDVEFPQ SNVPSVYDAL NVTDSKERLV LEVQQQLGGG VVRCIVMGSS
DGLRRGVEVV NTGAPISVPV GTKTLGRIMN VLGDAIDERG EVGAEEVYSI HRSAPSYEEQ
SNEIALLETG VKVIDLICPF AKGGKIGLFG GAGVGKTVNM MELINNIALQ HSGLSVFAGV
GERTREGNDF YYEMQEAGVV NVEKPEESKV AMVYGQMNEP PGNRLRVALT GLTMAERFRD
EGRDVLLFID NIYRYTLAGT EVSALLGRMP SAVGYQPTLA EEMGVLQERI TSTKSGSITS
VQAVYVPADD LTDPSPATTF AHLDATVVLN RNIAAMGLYP AIDPLDSTSR MLDPLVVGQD
HYEVARGVQQ TLQRYKELKD IIAILGMDEL SEEDKQVVSR ARKIERFLTQ PYHVAEVFTG
DPGIYVPLKE TLRGFKGLLA GEYDDIPEQA FMYCGSIDDA IENAKKL
