ID   HSCA_ECOL6              Reviewed;         616 AA.
AC   Q8FF44;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 98.
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=c3051;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81501.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN81501.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001196622.1; NC_004431.1.
DR   AlphaFoldDB; Q8FF44; -.
DR   SMR; Q8FF44; -.
DR   STRING; 199310.c3051; -.
DR   EnsemblBacteria; AAN81501; AAN81501; c3051.
DR   KEGG; ecc:c3051; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001410; 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..616
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_0000078627"
SQ   SEQUENCE   616 AA;  65592 MW;  2C17F724063AA4F4 CRC64;
     MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLADHEGR HLLPSVVHYQ
     QQGHSVGYDA RTNAALDTAN TISSVKRLMG RSLADIQQRY PHLPYQFQAS ENGLPMIETA
     AGLLNPVRVS ADILKALAAR ATEALAGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD
     FDHLLADYIR EQAGIPDRSD NRVQRELLDA AIAAKIALSD ADSVTVNVAG WQGEISREQF
     NELIAPLVKR TLLACRRALK DAGVEADEVL EVVVVGGSTR VPLVRERVGE FFGRPPLTSI
     DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA
     QDFTTFKDGQ TAMSIHVMQG ERELVQDCRS LARFALRGIP ALPAGGAHIR VTFQVDADGL
     LSVTAMEKST GVEASIQVKP SYGLTDSEIA SMIKDSMSYA EQDVKARMLA EQKVEAARVL
     ESLHGALAAD AALLSAAERQ AIDDAAAHLS EVAQGDDVDA IEQAIKNVDK QTQDFAARRM
     DQSVRRALKG HSVDEV