ATPB_EHRRW
ID ATPB_EHRRW Reviewed; 504 AA.
AC Q5HB71; Q5FEJ1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
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};
GN OrderedLocusNames=Erum4590, ERWE_CDS_04810;
OS Ehrlichia ruminantium (strain Welgevonden).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=254945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA Allsopp B.A.;
RT "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT tandem repeats of actively variable copy number.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Welgevonden;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI26975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR767821; CAH58187.1; -; Genomic_DNA.
DR EMBL; CR925678; CAI26975.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5HB71; -.
DR SMR; Q5HB71; -.
DR STRING; 254945.Erum4590; -.
DR EnsemblBacteria; CAI26975; CAI26975; ERWE_CDS_04810.
DR KEGG; eru:Erum4590; -.
DR KEGG; erw:ERWE_CDS_04810; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_5; -.
DR Proteomes; UP000001021; 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: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 Translocase; Transport.
FT CHAIN 1..504
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000254258"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 504 AA; 54843 MW; D73074F8F1EC8FCB CRC64;
MSSLTGKVKG RARKIKGDAD IRINESTENV GLVIRVMTAV VDIKFPSGKV PKILNALESK
EIYNGKKLVL EVSQHISDSI VRCIALDSTD GLSRNDEFID TGAPISVPVG RATLGRVFDV
LGNPIDNCGP LTKSDYSIKP IYSEVPKLTD QKVTTEILVT GIKVIDLLAP YLKGGKVGLF
GGAGVGKTVL IMELIHNIAK AHKGVSVFAG VGERTREGND LYHEMIESGV INLEEKDKSQ
AVLVYGQMNE PPGARLRVAL SALTMAEYFR DVENQDVLFF VDNIFRFTQS GSEISALLGR
IPSAVGYQPT LAAEMGAMQE RITSTNRGSI TSVQAIYVPA DDLTDPAPAT SFAHLDSTTV
LSRQIAELGI YPAVDPLDSA SQALSIDIVG EKHYEVSKEV QRILQTYKSL QDIIAILGME
ELSEEDKLIV ARARKIQRFL SQPFHVAEVF TGTPGVFVSL EDTVSSFKDI VEGKYDHLPE
AAFYMVSNIN EAVKKAELLQ KEGK
