ID   HSCA_RALSO              Reviewed;         621 AA.
AC   Q8Y0L9;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=RSc1024;
GN   ORFNames=RS04231;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646052; CAD14726.1; -; Genomic_DNA.
DR   RefSeq; WP_011000976.1; NC_003295.1.
DR   AlphaFoldDB; Q8Y0L9; -.
DR   SMR; Q8Y0L9; -.
DR   STRING; 267608.RSc1024; -.
DR   EnsemblBacteria; CAD14726; CAD14726; RSc1024.
DR   GeneID; 60500532; -.
DR   KEGG; rso:RSc1024; -.
DR   PATRIC; fig|267608.8.peg.1041; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001436; 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..621
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078642"
SQ   SEQUENCE   621 AA;  65945 MW;  1C9FAA6FF3BC4BEB CRC64;
     MALLQISEPG ESPAPHQRRL AVGIDLGTTN SLVAAVRSSV PEVLPDEQGR PLLPSVVRYL
     PAGGAQIGYK AQVEAVRDPK NTIVSVKRFM GRGLKDVAHI ENTPYDFVDA PGMVQLKTVA
     GVKSPVEVSA EILATLRQRA EDTLGDDLVG AVITVPAYFD DAQRQATKDA ARLAGLNVLR
     LLNEPTAAAI AYGLDNAAEG VYAVYDLGGG TFDISVLKLT KGVFEVMSTG GDSALGGDDF
     DQRIACWIVE QAGLQPLSAE DMRLLLNKAR AAKEWLSGAD STEVDAVLST GETVHLVLTA
     ETFAELTANL VQKTLAPVRR ALRDAGVAVD EIQGVVLVGG ATRMPVIRRA VAQLFGRAPL
     TNLDPDQVVA IGAAMQASLL AGNRAAGDDW LLLDVIPLSL GVETMGGLVE KIIPRNSTIP
     VARAQEFTTF KDGQTAMAIH VLQGERELAG DCRSLARFEL RGIPPMVAGA ARIRVTYQVD
     ADGLLSVSAR ETVSGVEASI AVKPSYGLGD DDIARMLQEG FQSAEEDMRR RALAEERVEG
     ERLLEALSHA LDADGDLLSA DERAAVDAQV AALRVTLQGE DHRAIKDAVD ALSHGTDEFA
     ARRMDRGIRA ALAGKRIEEL G