HSCA_EDWI9
ID HSCA_EDWI9 Reviewed; 616 AA.
AC C5BEU1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=NT01EI_3179;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR70329.1; -; Genomic_DNA.
DR RefSeq; WP_015872417.1; NC_012779.2.
DR AlphaFoldDB; C5BEU1; -.
DR SMR; C5BEU1; -.
DR STRING; 67780.B6E78_07555; -.
DR PRIDE; C5BEU1; -.
DR EnsemblBacteria; ACR70329; ACR70329; NT01EI_3179.
DR GeneID; 7958697; -.
DR KEGG; eic:NT01EI_3179; -.
DR PATRIC; fig|634503.3.peg.2840; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001485; 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_1000212529"
SQ SEQUENCE 616 AA; 65138 MW; 35A0FA01806BC4AA CRC64;
MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLADEQGH HLLPSVVRYQ
AGGHIVGAEA REQAADDPLN TVSSIKRMMG RSLADVQARY PHLPYQMHAS ESGMPQLATA
AGSVNPIQVS ADILAALSAR AQAALGGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
RLLNEPTAAA IAYGLDSAQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD
FDHLLADWLR EQAGLRDRSD AGLARRFLDA AVAAKIALST QQETTVCVGD WQGEVSRDQL
DALIAPLVKR TLLACHRTLK DAGVTRDEVL EVVMVGGSTR VPLVRTQVGD FFGRQPLTTI
DPDRVVAIGA AIQADILVGN KPDADMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA
QEFTTFKDGQ TAMMIHVLQG ERELVQDNRS LARFTLRGIP PLSAGGAHIR VTFQVDADGL
LSVTAMEKST GVQAAIQVKP SYGLSEDEIV GMLKDSMANA EGDLSARMLA EQKVEAARVL
ESLHGALQQD SALLGEQELA AIRQAQTALQ AAADGDETSA IEAAIKVLDA QTQEFAARRM
DSSIRRALAG HSVDEV
