HSCA_SALPK
ID HSCA_SALPK Reviewed; 616 AA.
AC B5BAX0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=SSPA0309;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(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}.
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DR EMBL; FM200053; CAR58426.1; -; Genomic_DNA.
DR RefSeq; WP_001196660.1; NC_011147.1.
DR AlphaFoldDB; B5BAX0; -.
DR SMR; B5BAX0; -.
DR KEGG; sek:SSPA0309; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000001869; 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_1000131692"
SQ SEQUENCE 616 AA; 65681 MW; 5F6F982D5C8C72B9 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 SYGLTDSEIA SMIKDSMSFA EQDVKARMLA EQKVEAARVL
ESLTGALTAD AALLSAAERQ CIDDAAAHLS AVAQGDDVDA IEQAIKNVDK QTQEFAARRM
DQSVRRALKG HSVDEV
