ID   HSCA_CUPPJ              Reviewed;         621 AA.
AC   Q473J2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Reut_A1063;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ60441.1; -; Genomic_DNA.
DR   RefSeq; WP_011297245.1; NC_007347.1.
DR   AlphaFoldDB; Q473J2; -.
DR   SMR; Q473J2; -.
DR   STRING; 264198.Reut_A1063; -.
DR   EnsemblBacteria; AAZ60441; AAZ60441; Reut_A1063.
DR   KEGG; reu:Reut_A1063; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
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..621
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044879"
SQ   SEQUENCE   621 AA;  66556 MW;  2D1A56D97FF0A932 CRC64;
     MALLQISEPG MSPAPHQRRL AVGIDLGTTN SLVAAVRNSI PEVLGDERGR ALLPSVVRYL
     PDRTTHIGYR AQDEAVRDPK NTIVSVKRFM GRGLKDVAHN EHSPYDFVDA PGMVQIKTVA
     GVKSPVEVSA EILATLRQRA EDSLGDDLVG AVITVPAYFD EAQRQATKDA ARLAGLEVLR
     LLNEPTAAAI AYGLDNASEG IYAVYDLGGG TFDISILKLT KGVFEVLSTG GDSALGGDDF
     DQRLLCWIVE QAGLQPLSAQ DMRLLMVRAR AAKEALSEGD STVIDAVLDS GEIVHLTLTD
     EIFDTITAHL VQKTLAPVRK ALRDAGVTPD EVQGVVLVGG ATRMPAIRKA VGDFFGQPPL
     TNLDPDRVVA LGAAMQANLL AGNHAPGEDW LLLDVIPLSL GVETMGGLVE KIIPRNSTIP
     VARAQEFTTF KDGQTAMAIH VLQGERELAS DCRSLARFEL RGIPPMVAGA ARIRVTYQVD
     ADGLLSVTAR ETHSGVESSV TVKPSYGLAD DDIARMLQEG FREAEHDMKS RALAEERVEA
     DRLVEATTRA LETDGDLLSA DERAAVEALI ASVREIATGE DHHAIKAAVE TLSRGTDEFA
     ARRMDRSIKS ALAGRKVQEL G