HSCA_PSEE4
ID HSCA_PSEE4 Reviewed; 620 AA.
AC Q1IEI8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PSEEN1014;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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. {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; CT573326; CAK13917.1; -; Genomic_DNA.
DR RefSeq; WP_011532340.1; NC_008027.1.
DR AlphaFoldDB; Q1IEI8; -.
DR SMR; Q1IEI8; -.
DR STRING; 384676.PSEEN1014; -.
DR EnsemblBacteria; CAK13917; CAK13917; PSEEN1014.
DR KEGG; pen:PSEEN1014; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000658; 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; 2.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Stress response.
FT CHAIN 1..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044871"
SQ SEQUENCE 620 AA; 65850 MW; 28DDD7C909837E3A CRC64;
MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVAALRSGR SEPLPDAQGN VILPSAVRYL
ANGVEVGLGA REAAPSDPLN SILSVKRLMG RGLADVKQLG EQLPYRFVGG ESHMPFIDTV
QGPKSPVEVS ADILKVLRQR AEDTLGGELV GAVITVPAYF DDAQRQATKD AAKLAGLNVL
RLLNEPTAAA VAYGLDQHAE GVVAIFDLGG GTFDISILRL TAGVFEVLAT GGDTALGGDD
FDHAIAGWII EQAGLSADLD PATQRLLLQT ACAAKEALTD SEAVSVQHGA WQGELTRGAF
EAMIEPMIAR SLKACRRAVR DSGIELEEVG AVVMVGGSTR VPRVREAVGS LFGRTPLTSI
DPDQVVAIGA AIQADTLAGN RREGGELLLL DVIPLSLGLE TMGGLMEKVI PRNTTIPVAR
AQEFTTYKDG QSAMMIHVLQ GERELISDCR SLARFELRGI PAMVAGAAKI RVTFQVDADG
LLSVAARELG SGVESSIQVK PSYGLTDGEI ARMLKDSFEH AGADKHARQL REHQVDAERL
LEAVQGALDA DGERLLSDDE REAIAFQMQE LRDLLTGTDG AAIEQQTKRL SQVTDAFAAR
RLDSTVKAAL AGRNLNEIEE
