ID   HSCA_PROMH              Reviewed;         616 AA.
AC   B4EZU4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=PMI1856;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR43848.1; -; Genomic_DNA.
DR   RefSeq; WP_012368127.1; NC_010554.1.
DR   AlphaFoldDB; B4EZU4; -.
DR   SMR; B4EZU4; -.
DR   STRING; 529507.PMI1856; -.
DR   EnsemblBacteria; CAR43848; CAR43848; PMI1856.
DR   GeneID; 6801330; -.
DR   KEGG; pmr:PMI1856; -.
DR   PATRIC; fig|529507.6.peg.1808; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000008319; 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; Reference proteome.
FT   CHAIN           1..616
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_1000131683"
SQ   SEQUENCE   616 AA;  66635 MW;  4117D2B2E43CF588 CRC64;
     MSLLQISEPG QTPAPHQRRL AAGIDLGTTH SLVATVRSGQ AEALSDSEGR YLLPSVVQYQ
     VDNINVGWQA KQEAEKDPAN TISSIKRMLG RSLNDITSRY PNLPYHFHDN DSGLPLIKTP
     AGIVDPIQVS ADILKALAER AIQSLGGELD GVVVTVPAYF DDAQRQGTKE AARRAGLHVL
     RLLNEPTAAA IAYGLDSGKE GTIVVYDLGG GTFDISVLRL TKGVFEVLAT GGDTALGGDD
     FDMMLADWIR ERAGFGYQND VILQRQLLDI ASETKIALSD NDVADINING WKGEITRAEF
     ELLIQPLVKR TLLSVRRALK DADVDVDEVL EVVMVGGSTR VPLVRQMVGD YFKREPLTSI
     DPDKVVAIGA SIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA
     QEFTTFKDGQ TAMSVHVVQG EREMVSDCRS LARFTLRGIP PMAAGGAHIR VTFQVDADGL
     LSVSAMEKST GVEASVQVKP SYGLSDTEIA NMIQSSMENA KEDLQARRLA EQKVEAARVL
     ESLTAALQED AHLLTEDEKT AIDNVVDTLI ESVEGTDPVA IENAIKQLDK QTQEFAARRM
     DTSIRQALAG HSVDEI