ID   HSCA_ACISJ              Reviewed;         622 AA.
AC   A1W7T4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Ajs_2140;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000539; ABM42309.1; -; Genomic_DNA.
DR   RefSeq; WP_011805371.1; NC_008782.1.
DR   AlphaFoldDB; A1W7T4; -.
DR   SMR; A1W7T4; -.
DR   STRING; 232721.Ajs_2140; -.
DR   PRIDE; A1W7T4; -.
DR   EnsemblBacteria; ABM42309; ABM42309; Ajs_2140.
DR   KEGG; ajs:Ajs_2140; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_4; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000000645; 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_1000044838"
SQ   SEQUENCE   622 AA;  65448 MW;  7E59FC0BBEE78F75 CRC64;
     MALLQISEPG QSPDPHQRRV AIGIDLGTTH SLVAAVRNGV AECLPDAQGR VLLPSVVRYL
     GGGGRQIGYE AAAAQMQDPA NTVSSVKRFM GRGLGDITGR EKLPYNFIAA TDSGGMLSLS
     TAAGVKSPVE VSAEILATLR YRAEDSFDSD LYGAVITVPA YFDDAQRQAT KDAAHLAGLN
     LLRLINEPTA AAIAYGLDNG AEGVYAVYDL GGGTFDISVL RLAQGVFEVI ATGGDSALGG
     DDYDAALAEW VMQQTGVRAS TPEDKTAVRL AARACKEALT ATDNVAFTAD VAGATVQFDV
     KREDFAAVTA DLTQRSLAAV RRTLRDAQIE RDEVKGVVLV GGSTRMPVVR TAVAEFFGRE
     PLTNLNPDEV VAIGAAIQAN QLAGNDAAGD LLLLDVIPLS LGIETMGGLV ERIIGRNETI
     PTAKAQDFTT YKDGQTALAI HVVQGERDLV QDCRSLARFE LRGIPPMAAG AARIRVTFTV
     DADGLLSVAA REQASGVEAR IDVKPSYGLT DEQIARMLQE GFATAQQDMQ TRALVEARVD
     ADRLLIATQS ALDVDGDVLT AAERTAIDDL MHALRATLET STDAAAVEAA AQALAKGTEA
     FAAQRMNRGI RQALAGKNVS AL