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ATPB_GLUDA
ID   ATPB_GLUDA              Reviewed;         493 AA.
AC   A9H9A8; B5ZHL5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=GDI0696, Gdia_1313;
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS   / CIP 103539 / LMG 7603 / PAl5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA   Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA   Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA   Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA   Figueiredo D., Montano H., Junior J., de Souza Filho G.,
RA   Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P.,
RA   Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA   Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA   Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA   Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O.,
RA   Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX   PubMed=21304715; DOI=10.4056/sigs.972221;
RA   Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT   "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT   diazotrophicus PAl 5, suggest a new standard in genome sequence
RT   submission.";
RL   Stand. Genomic Sci. 2:309-317(2010).
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; AM889285; CAP54639.1; -; Genomic_DNA.
DR   EMBL; CP001189; ACI51095.1; -; Genomic_DNA.
DR   RefSeq; WP_012223291.1; NC_011365.1.
DR   AlphaFoldDB; A9H9A8; -.
DR   SMR; A9H9A8; -.
DR   STRING; 272568.GDI0696; -.
DR   PRIDE; A9H9A8; -.
DR   EnsemblBacteria; ACI51095; ACI51095; Gdia_1313.
DR   EnsemblBacteria; CAP54639; CAP54639; GDI0696.
DR   KEGG; gdi:GDI0696; -.
DR   KEGG; gdj:Gdia_1313; -.
DR   eggNOG; COG0055; Bacteria.
DR   HOGENOM; CLU_022398_0_2_5; -.
DR   OMA; GFNMIMD; -.
DR   OrthoDB; 430176at2; -.
DR   Proteomes; UP000000736; Chromosome.
DR   Proteomes; UP000001176; 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   Reference proteome; Translocase; Transport.
FT   CHAIN           1..493
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000339530"
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   493 AA;  52874 MW;  6917E5D35680FF3F CRC64;
     MSETTQNEAP VAAQGASQHS NIVGRVTQVR GAVVDVQFEG TLPHILDALH VTFNGQTVVL
     EVAQEIGEHE VRCIAMDTTD GLMRGTEVVA TGGQITVPVG PGTLGRILNV IGEPIDERGP
     VKSDKRYPIH RKAPSFDEQA AATEILVTGI KVVDLLCPYL KGGKVGLFGG AGVGKTVIIQ
     ELINNIAKAH GGVSVFAGVG ERTREGNDLY YEMQDAGVIK LGEDTTEGSK VALVYGQMNE
     PPGARARIAL SGLSLAEYFR DEEGQDVLFF VDNIFRFTQA GAEVSALLGR IPSAVGYQPT
     LATEMGALQE RITSTKKGSI TSVQAVYVPA DDLTDPAPAA TFAHLDATTV LNRSIAEMGI
     YPAVDPLDST SRSLDPKIVG EEHYQVARDV QRILQTYKSL QDIIAILGMD ELSEDDKQVV
     ARARRIQRFL SQPFHVAEVF TGAPGKLVSL EDTVRSFKAI VAGEYDHLPE GAFYMVGSIE
     EAVAKAEKMK ETA
 
 
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