ID   HSCA_SALNS              Reviewed;         616 AA.
AC   B4T0R8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, 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=SNSL254_A2738;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001113; ACF61310.1; -; Genomic_DNA.
DR   RefSeq; WP_001196659.1; NZ_CCMR01000001.1.
DR   AlphaFoldDB; B4T0R8; -.
DR   SMR; B4T0R8; -.
DR   EnsemblBacteria; ACF61310; ACF61310; SNSL254_A2738.
DR   KEGG; see:SNSL254_A2738; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000008824; 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_1000131691"
SQ   SEQUENCE   616 AA;  65651 MW;  29B4F580EA5C33AD CRC64;
     MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLPDHEGR HLLPSVVHYQ
     QQGHTVGYAA RDNAAQDTAN TISSVKRMMG RSLADIQARY PHLPYRFKAS VNGLPMIDTA
     AGLLNPVRVS ADILKALAAR ASESLSGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
     RLLNEPTAAA IAYGLDSGKE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD
     FDHLLADYIR EQAGIADRSD NRVQRELLDA AITAKIALSD ADTVRVNVAG WQGEITREQF
     NDLISALVKR TLLACRRALK DAGVEPQDVL EVVMVGGSTR VPLVRERVGE FFGRTPLTAI
     DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA
     QDFTTFKDGQ TAMSIHVMQG ERELVQDCRS LARFALRGIP PLPAGGAHIR VTFQVDADGL
     LSVTAMEKST GVEASIQVKP SYGLTDGEIA SMIKDSMSFA EQDVKARMLA EQKVEAARVL
     ESLTGALTAD AALLSAAERQ CIDDAAAHLS AVAQGDDVDA IEQAIKNVDK QTQEFAARRM
     DQSVRRALKG HSVDEV