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ATPB_SYNJB
ID   ATPB_SYNJB              Reviewed;         477 AA.
AC   Q2JIV9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
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   Synonyms=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
GN   OrderedLocusNames=CYB_2502;
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13);
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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 four main
CC       subunits: a(1), b(1), b'(1) and c(9-12). {ECO:0000255|HAMAP-
CC       Rule:MF_01347}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid 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; CP000240; ABD03435.1; -; Genomic_DNA.
DR   RefSeq; WP_011434062.1; NC_007776.1.
DR   AlphaFoldDB; Q2JIV9; -.
DR   SMR; Q2JIV9; -.
DR   STRING; 321332.CYB_2502; -.
DR   KEGG; cyb:CYB_2502; -.
DR   eggNOG; COG0055; Bacteria.
DR   HOGENOM; CLU_022398_0_2_3; -.
DR   OMA; GFNMIMD; -.
DR   OrthoDB; 430176at2; -.
DR   Proteomes; UP000001938; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid 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; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Nucleotide-binding; Reference proteome; Thylakoid; Translocase;
KW   Transport.
FT   CHAIN           1..477
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000254407"
FT   BINDING         163..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   477 AA;  51471 MW;  1152907BEBFD0335 CRC64;
     MVTATATATN VGYITQVIGP VIDAEFPSGK LPEIYNALKV EGTTESGLKV NVTFEVQQLL
     GDNRVRAVAM SSTDGLVRGM PVVDTGAPIT VPVGQPTLGR IFNVLGEPVD QGEPVQAQEF
     APIHRSAPPL VDLTIKPEPF ETGIKVIDLL APFKKGGKVG LFGGAGVGKT VLIQELIHNI
     AEEHSGLSVF AGVGERTREG NDLYNEMKES GVLDKVALVY GQMNEPPGAR MRVGLTALTM
     AEYFRDVNKQ DVLLFIDNIF RFVQAGSEVS ALLGRMPSAV GYQPTLATEM GNLQERITST
     KQGSITSVQA VYVPADDLTD PAPATTFAHL DSTVVLSRSL AAKGIYPAVD PLDSSSTILQ
     ADIVGEEHYN TARAVKQTLQ RYKELQDIIA ILGLDELSEE DKLVVARARR IERFLSQPFF
     VAEVFTGSPG KYVKLADTIK GFQRILSGEL DNLPEQAFYL VGTIEEAIEK AEKLKSK
 
 
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