HSCA_ECOLC
ID HSCA_ECOLC Reviewed; 616 AA.
AC B1IWD5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=EcolC_1151;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) 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; CP000946; ACA76818.1; -; Genomic_DNA.
DR RefSeq; WP_001196613.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IWD5; -.
DR SMR; B1IWD5; -.
DR GeneID; 67416910; -.
DR KEGG; ecl:EcolC_1151; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
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_1000082981"
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
