ID   HSCA_CUPTR              Reviewed;         621 AA.
AC   B3R475;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=RALTA_A1144;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ69108.1; -; Genomic_DNA.
DR   RefSeq; WP_012352436.1; NC_010528.1.
DR   AlphaFoldDB; B3R475; -.
DR   SMR; B3R475; -.
DR   STRING; 977880.RALTA_A1144; -.
DR   PRIDE; B3R475; -.
DR   EnsemblBacteria; CAQ69108; CAQ69108; RALTA_A1144.
DR   GeneID; 29761991; -.
DR   KEGG; cti:RALTA_A1144; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; CTAI977880:RALTA_RS05460-MON; -.
DR   Proteomes; UP000001692; Chromosome 1.
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_1000131670"
SQ   SEQUENCE   621 AA;  66648 MW;  B99AE9C44609161E CRC64;
     MALLQISEPG MSPAPHQRRL AVGIDLGTTN SLVAAVRSSI PEVLADERGR ALLPSVVRYL
     PDRTAQIGYR AQDEAVRDPK NTIVSVKRFM GRGLRDVANI EHSPYDFVDA PGMVQIKTAA
     GVKSPVEISA EILATLRQRA EDSLGDDLVG AVITVPAYFD EAQRQATKDA ARLAGLEVLR
     LLNEPTAAAI AYGLDNAAEG IYAVYDLGGG TFDISVLKLT QGVFEVLATG GDSALGGDDF
     DQRLLCWIVE QANLQPLSAQ DMRLLMVRAR AAKEALSEAD STVIDAVLES GEIVHLTLTD
     EIFEQITAHL VQKTLAPVRK ALRDAGVGPE EVKGVVLVGG ATRMPSIRKA VGDFFGQNPL
     TNLDPDRVVA LGAAMQANLL AGNHAPGEDW LLLDVIPLSL GVETMGGLVE KIIPRNSTIP
     VARAQEFTTF KDGQTAMAIH VLQGERELAS DCRSLARFEL RGIPPMVAGA ARIRVTYQVD
     ADGLLSVTAR ETHSGVEASV TVKPSYGLAD DDIARMLQDS FREAEHDMKS RALAEERVEA
     DRLVEATQRA LETDGDLLSA DERAAVEALM ATVREIATGE DHLAIRAAVE KLSHGTDEFA
     ARRMDRSIKS ALAGRKVQEL G