ATPB_HELPY
ID ATPB_HELPY Reviewed; 469 AA.
AC P55988; O07676;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
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}; OrderedLocusNames=HP_1132;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=9199431; DOI=10.1128/iai.65.7.2640-2647.1997;
RA McGowan C.C., Cover T.L., Blaser M.J.;
RT "Analysis of F1F0-ATPase from Helicobacter pylori.";
RL Infect. Immun. 65:2640-2647(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AF004014; AAB61298.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD08174.1; -; Genomic_DNA.
DR PIR; D64661; D64661.
DR RefSeq; NP_207923.1; NC_000915.1.
DR RefSeq; WP_000646366.1; NC_018939.1.
DR AlphaFoldDB; P55988; -.
DR SMR; P55988; -.
DR DIP; DIP-3361N; -.
DR IntAct; P55988; 2.
DR MINT; P55988; -.
DR STRING; 85962.C694_05840; -.
DR PaxDb; P55988; -.
DR EnsemblBacteria; AAD08174; AAD08174; HP_1132.
DR KEGG; hpy:HP_1132; -.
DR PATRIC; fig|85962.8.peg.1184; -.
DR eggNOG; COG0055; Bacteria.
DR OMA; GFNMIMD; -.
DR PhylomeDB; P55988; -.
DR Proteomes; UP000000429; 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); IBA:GO_Central.
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 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..469
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144444"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT VARIANT 73..74
FT /note="VI -> AV (in strain: CCUG 17874 / NCTC 11638)"
FT VARIANT 363
FT /note="V -> I (in strain: CCUG 17874 / NCTC 11638)"
SQ SEQUENCE 469 AA; 51478 MW; CEF654B885738181 CRC64;
MKAMEGKIIQ VLGPVVDVEF ESYLPAIFEA LDINFEVNGV QKSLVLEVAA HLGGNRVRAI
AMDMTEGLVR NQVIKARGKM IEVPVGEEVL GRIFNVVGES IDNLEPLKPS LTWPIHRKAP
SFEQQSTKTE MFETGIKVID LLAPYSKGGK VGLFGGAGVG KTVIIMELIH NVAYKHNGYS
VFAGVGERTR EGNDLYFEMK EGGVLDKVAL CYGQMNEPPG ARNRIAFTGL TMAEYFRDEK
GLDVLMFIDN IFRYAQSGAE MSALLGRIPS AVGYQPTLAG EMGKLQERIA STKNGSITSV
QAVYVPADDL TDPAPASVFA HLDATTVLNR KIAEKGIYPA VDPLDSTSRI LSPQMIGEKH
YEVATGIQQV LQKYKDLQDI IAILGLDELS EEDKKTVERA RKIEKFLSQP FFVAEVFTGS
PGKYVTLQET LEGFGGILEG KYDHIPENAF YMVGSIQEVL EKAKNMKNS
