ID   HSCA_YERPS              Reviewed;         644 AA.
AC   Q667Y5;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Chaperone protein HscA {ECO:0000255|HAMAP-Rule:MF_00679};
DE   AltName: Full=Hsc66 {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=YPTB2855;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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. Involved in the maturation of IscU.
CC       {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; BX936398; CAH22093.1; -; Genomic_DNA.
DR   RefSeq; WP_011192811.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q667Y5; -.
DR   SMR; Q667Y5; -.
DR   EnsemblBacteria; CAH22093; CAH22093; YPTB2855.
DR   GeneID; 66844723; -.
DR   KEGG; ypo:BZ17_3776; -.
DR   KEGG; yps:YPTB2855; -.
DR   PATRIC; fig|273123.14.peg.3962; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001011; 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; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..644
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_0000078658"
SQ   SEQUENCE   644 AA;  68486 MW;  429E7E4949E7FA24 CRC64;
     MALLQISEPG LTAAPHQRRL AAGIDLGTTN SLVATVRSGK AQTLADEQLA DEQLIAGEQL
     IAGEQLIAGQ QLINEKQRDL LPSVVHYHPQ GIDVGWKARN LAALDPVNTI SSVKRMMGRS
     LADIVQRYPN LPYQFHASEN GLPMIQTARG LVNPVQVSAE ILKTLAQRAQ AALAGELDGV
     VITVPAYFDD AQRQGTKDAA RLAGLHVLRL LNEPTAAAIA YGLDSGQEGV IAVYDLGGGT
     FDISILRLSR GVFEVLATGG DSALGGDDFD HLLADWLREQ AGVATRDDHG IQRQLLDTAI
     AAKIALSEAE TAVVSVAGWQ GEVTREQLES LIAPLVKRTL MACRRALKDA GVTADEILEV
     VMVGGSTRVP LVREQVGQFF GRTPLTSIDP DKVVAIGAAI QADILVGNKP DSDMLLLDVI
     PLSLGLETMG GLVEKVIPRN TTIPAARAQE FTTFKDGQSA MMIHVLQGER ELVKDCRSLA
     RFTLRGLPPL PAGGAHIRVT FQVDADGLLS VTAMEKSTGV EASIQVKPSY GLSDDEIANM
     IKDSMANAQS DITARKLAEQ QVDAARVLES LQGALAEDAA LLSEQESAAI AQAVALLQQQ
     MQGSDPQAIE AATKALDAQT QDFAARRMDA SIRRALAGHS VDEV