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HSCA_PSESM
ID   HSCA_PSESM              Reviewed;         620 AA.
AC   Q886Z7;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PSPTO_1427;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC   -!- FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster-
CC       containing proteins. Has a low intrinsic ATPase activity which is
CC       markedly stimulated by HscB. {ECO:0000255|HAMAP-Rule:MF_00679}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00679}.
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DR   EMBL; AE016853; AAO54948.1; -; Genomic_DNA.
DR   RefSeq; NP_791253.1; NC_004578.1.
DR   RefSeq; WP_011103546.1; NC_004578.1.
DR   AlphaFoldDB; Q886Z7; -.
DR   SMR; Q886Z7; -.
DR   STRING; 223283.PSPTO_1427; -.
DR   EnsemblBacteria; AAO54948; AAO54948; PSPTO_1427.
DR   GeneID; 1183064; -.
DR   KEGG; pst:PSPTO_1427; -.
DR   PATRIC; fig|223283.9.peg.1447; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   PhylomeDB; Q886Z7; -.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd10236; HscA_like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00679; HscA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR042039; HscA_NBD.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR010236; ISC_FeS_clus_asmbl_HscA.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01991; HscA; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078641"
SQ   SEQUENCE   620 AA;  66370 MW;  2362340E256AA93C CRC64;
     MALLQIAEPG LSPQPHQRRL AVGIDLGTTN SLVAAVRSGL SEPLADAEGQ VILPSAVRYH
     ADRVEVGQAA KAAASQDPFN TVLSVKRLMG RGLSDVKQLG EQLPYRFVGG ESHMPFIDTV
     QGAKSPVEVS ADILKVLRQR AEAALGGELV GAVITVPAYF DDSQRQATKD AAKLAGLNVL
     RLLNEPTAAA VAYGLDQKAE GVIAIYDLGG GTFDISILRL TGGVFEVLAT GGDTALGGDD
     FDHAIASWIV ADAGLSADLD PSAQRSLLQA ACSAKEALTD AEFVEVTHGE WRGTLTRDAL
     NALIEPMIAR SLKACRRAVR DTGIELEEVE AVVMVGGSTR VPRVREAVAE LFGRQPLTQI
     DPDQVVAIGA AIQADTLAGN KRDGGELLLL DVIPLSLGLE TMGGLMEKVI PRNTTIPVAR
     GQEFTTYKDG QTAMKIHVLQ GERELVSDCR SLARFELRGI PPMVAGAAKI RVTFQVDADG
     LLSVSAREMG SGIESSIQVK PSYGLTDDEV TRMLKDSFEY AGDDKVARVL REHQVDAERL
     LEAVQGALDA DGERLLDEEE RLVINLQMDE LRELMQGTDG YAIEQQTKRL SQVTDAFAAR
     RLDSTVKAAL AGRNLNEIEE
 
 
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