HSCA_PECCP
ID HSCA_PECCP Reviewed; 616 AA.
AC C6DBI7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=PC1_3027;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-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; CP001657; ACT14050.1; -; Genomic_DNA.
DR RefSeq; WP_015841202.1; NC_012917.1.
DR AlphaFoldDB; C6DBI7; -.
DR SMR; C6DBI7; -.
DR STRING; 561230.PC1_3027; -.
DR EnsemblBacteria; ACT14050; ACT14050; PC1_3027.
DR KEGG; pct:PC1_3027; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002736; 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_1000212530"
SQ SEQUENCE 616 AA; 65733 MW; F3455579FA118699 CRC64;
MALLQISEPG LSAAPHQRRL AVGIDLGTTH SLVATVRSGE AQTLVDSDGR DLLPSVVHYR
RDGHSVGWQA RDNAARDPEN TVSSVKRLMG RSLDDIQQRY PHLPYRFHAS DNGLPLIQTP
AGNLNPIQVS ADILSALAAR AEAALGGVPD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
RLLNEPTAAA IAYGLDSGKE GVIAIYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD
FDHLLAEWLR EQAGIHDRDD RQLDHALRAA AVKAKIALSS AESASVSIAG WQGDITREQF
DSLIAPLVKR TLLSCRRTLK DAGLTPEEVL EVVMVGGSTR VPLVREQVGT FFGRTPLTSI
DPDKVVAMGA AIQADILVGN KPDSDMLLLD VIPLSLGLET MGGLVEKIIP RNTTIPVARA
QEFTTFKDGQ SGMMIHVLQG EREMVADCRS LARFSLRGLP PLPAGGAHIR VTFQVDADGL
LSVTAMEKST GVEASIQVKP SYGLSDTEIA TMITDSMLNA KEDVGARRLA EQKVEAARVL
ESLQSALVAD AELLSNDEKG VIVAASEHLH TMMQGSDPVA IEAAIKTVDQ QTQEFAARRM
DASIRRALAG HSVDEV
