ID   HSCA_CUPNH              Reviewed;         621 AA.
AC   Q0KCG7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=H16_A1163;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(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}.
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; AM260479; CAJ92304.1; -; Genomic_DNA.
DR   RefSeq; WP_010809021.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q0KCG7; -.
DR   SMR; Q0KCG7; -.
DR   STRING; 381666.H16_A1163; -.
DR   EnsemblBacteria; CAJ92304; CAJ92304; H16_A1163.
DR   GeneID; 57643260; -.
DR   KEGG; reh:H16_A1163; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008210; 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; Reference proteome.
FT   CHAIN           1..621
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044878"
SQ   SEQUENCE   621 AA;  66712 MW;  94AF8D23EAFF902B CRC64;
     MALLQISEPG MSPAPHQRRL AVGIDLGTTN SLVAAVRSSI PEVLGDERGR ALLPSVVRYL
     PDRTAHIGYR AQEEAVRDPK NTIVSVKRFM GRGLRDVANI EHSPYDFVDA PGMLQIKTAA
     GVKSPVEISA EILATLRQRA EDTLGDDLVG AVITVPAYFD EAQRQATKDA ARLAGLEVLR
     LLNEPTAAAI AYGLDNASEG IYAVYDLGGG TFDISVLKLT QGVFEVLATG GDSALGGDDF
     DQRLLCWIVE QASLQPLSAQ DMRLLMVRAR AAKEALSESD STVIDAVLES GEIVHLTLTV
     EIFDQVTAHL VQKTLAPVRK ALRDAGVAPD EVKGVVLVGG ATRMPSIRKA VGDYFGQTPL
     TNLDPDRVVA LGAAMQANLL AGNHAPGEDW LLLDVIPLSL GVETMGGLVE KIIPRNSTIP
     VARAQEFTTF KDGQTAMAIH VLQGERELAS DCRSLARFEL RGIPPMVAGA ARIRVTYQVD
     ADGLLSVTAR ETHSGVEASV TVKPSYGLAD DDIARMLQES FREAEHDMKS RALAEERVEA
     DRLVEATQRA LETDGDLLSA EERTAVEALM ATVREIATGE DHHAIHAAVE KLSHGTDEFA
     ARRMDRSIKS ALAGRKVQEL G