ID   HSCA_AZOSB              Reviewed;         622 AA.
AC   A1K724;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=azo2012;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(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}.
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DR   EMBL; AM406670; CAL94629.1; -; Genomic_DNA.
DR   RefSeq; WP_011765743.1; NC_008702.1.
DR   AlphaFoldDB; A1K724; -.
DR   SMR; A1K724; -.
DR   STRING; 62928.azo2012; -.
DR   PRIDE; A1K724; -.
DR   EnsemblBacteria; CAL94629; CAL94629; azo2012.
DR   KEGG; azo:azo2012; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002588; 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..622
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044842"
SQ   SEQUENCE   622 AA;  66515 MW;  DD06028BE60539CE CRC64;
     MALLQIAEPG MSAEPHKHRL AVGIDLGTTN SLVATVRNGL SVCLADEEGR AMLPSIVRYR
     ADGAVQVGHA AAPFQATDPK NTIVSAKRFM GRGLKDVAYV EAMPYDFEDA PGMVRLRTVQ
     GVKSPVEVSA EILRALRERA EASLGGPLTG AVITVPAYFD DAQRQATKDA ARLAGLEVLR
     LLNEPTAAAV AYGLDNAAEG VYAVYDLGGG TFDLSVLKLS RGVFEVLSTN GDAALGGDDF
     DHRLFCWVLD KARIAPPSTE DARRLQLKAR EAKELLTACE SAQIQCRLAS GEEVDLVVTR
     EAFAEMTAHL VKKTLGPVRK ALRDAGLAPE DIKGVVMVGG ATRMPHIQRA VAEYFGQEPL
     NNLDPDKVVA LGAAIQANVL AGNRASEDDW LLLDVIPLSL GLETMGGLVE KVVPRNSTLP
     IARAQEFTTF KDGQTAMAFH VVQGERELVA DCRSLARFEL RGIPPMAAGA ARIRVTFQVD
     ADGLLSVSAR EMSSGVEASV LVKPSYGLSD DEISGMLREG MERAGDDMAA RALREQQVEA
     DRVIEATEHA LAADGSLLNA EERASIDAAI DALRALRAGT DHRAIKAGID ALSRATDEFA
     ARRMDHSIRA ALTGHKLDEF QT