ID   HSCA_ECO55              Reviewed;         616 AA.
AC   B7LDB8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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};
GN   OrderedLocusNames=EC55989_2811;
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928145; CAU98684.1; -; Genomic_DNA.
DR   RefSeq; WP_001196613.1; NC_011748.1.
DR   AlphaFoldDB; B7LDB8; -.
DR   SMR; B7LDB8; -.
DR   EnsemblBacteria; CAU98684; CAU98684; EC55989_2811.
DR   GeneID; 67416910; -.
DR   KEGG; eck:EC55989_2811; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000000746; 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_1000147715"
SQ   SEQUENCE   616 AA;  65652 MW;  9C80E6EF1BFDAB48 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 EVVMVGGSTR VPLVRERVGE FFGRPPLTSI
     DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA
     QDFTTFKDGQ TAMSIHVMQG ERELVQDCRS LARFALRGIP ALPAGGAHIR VTFQVDADGL
     LSVTAMEKST GVEASIQVKP SYGLTDSEIA SMIKDSMSYA EQDVKARMLA EQKVEAARVL
     ESLHGALAAD AALLSAAERQ VIDDAAAHLS EVAQGDDVDA IEQAIKNVDK QTQDFAARRM
     DQSVRRALKG HSVDEV