ID   HSCA_CUPMC              Reviewed;         621 AA.
AC   Q1LPL1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Rmet_1029;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000352; ABF07915.1; -; Genomic_DNA.
DR   RefSeq; WP_011515822.1; NC_007973.1.
DR   AlphaFoldDB; Q1LPL1; -.
DR   SMR; Q1LPL1; -.
DR   STRING; 266264.Rmet_1029; -.
DR   EnsemblBacteria; ABF07915; ABF07915; Rmet_1029.
DR   KEGG; rme:Rmet_1029; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002429; 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_1000044880"
SQ   SEQUENCE   621 AA;  66246 MW;  9A4B3E9F05405A52 CRC64;
     MALLQISEPG MSPAPHQRRL AVGIDLGTTN SLVAAVRNSI PEVLPDEHGR ALLPSVVRYL
     PNGNAHIGYK AQDEAVRDPK NTIISVKRFM GRGVRDVANI EHSLYDFVDA PGMVQLKTAA
     GIKSPVEVSA EILATLRQRA EDSLGDELVG AVITVPAYFD DAQRQATKDA AQLAGLEVLR
     LLNEPTAAAI AYGLDNAAEG IYAVYDLGGG TFDISVLKLT KGVFEVMSTG GDSALGGDDF
     DQRLLCWIVE QVGLQPLSAE DSRLLMVRAR AAKEALSSSD STVIDAVLTS GEIVHLTLDA
     DTFIQITANL VQKTLTPVRK ALRDAGVGPE DVKGVVLVGG ATRMPAIRKA VGDYFGQQPL
     TNLDPDRVVA LGAAMQANLL AGNHAPGEDW LLLDVIPLSL GVETMGGLVE KIVPRNSTIP
     VARAQEFTTF KDGQTAMAIH VLQGERELAS DCRSLARFEL RGIPPMVAGA ARIRVTYQVD
     ADGLLSVSAR ETGSGVEASV SVKPSYGLAD DDIARMLQES FQEAEHDMKN RALAEERVEA
     ARLVEATTRA LETDGNLLSA DERAAVDELM ANVSEIAKGE DHRAIKAAVE RLSQGTDEFA
     ARRMDRSIKS ALAGKKVQEI G