ID   HSCA_ACIET              Reviewed;         622 AA.
AC   B9MIT4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Dtpsy_1642;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Diaphorobacter.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) 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; CP001392; ACM33100.1; -; Genomic_DNA.
DR   RefSeq; WP_015913192.1; NC_011992.1.
DR   AlphaFoldDB; B9MIT4; -.
DR   SMR; B9MIT4; -.
DR   STRING; 535289.Dtpsy_1642; -.
DR   EnsemblBacteria; ACM33100; ACM33100; Dtpsy_1642.
DR   KEGG; dia:Dtpsy_1642; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000450; 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.
FT   CHAIN           1..622
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000147713"
SQ   SEQUENCE   622 AA;  65375 MW;  CE9E0CFE7569B717 CRC64;
     MALLQISEPG QSPDPHQRRV AIGIDLGTTH SLVAAVRNGV AECLPDAQGR VLLPSVVRYL
     GGGGRQIGYE AAAAQMQDPA NTVSSVKRFM GRGLGDITGR EKLPYDFIAA ADSGGMLSLS
     TAAGVKSPVE VSAEILATLR YRAEDSFDSD LYGAVITVPA YFDDAQRQAT KDAAHLAGLN
     LLRLINEPTA AAIAYGLDNG AEGVYAVYDL GGGTFDISVL RLAQGVFEVI ATGGDSALGG
     DDYDAALAEW VMQQTGVRAS TPEDKTSVRL AARACKEALT ATDNVAFTAD VAGATVQFDV
     KREDFAAVTA ELTQRSLAAV RRTLRDAQIE RDEVKGVVLV GGSTRMPVVR AAVAEFFGRE
     PLTNLNPDEV VAIGAAIQAN QLAGNDAAGD LLLLDVIPLS LGIETMGGLV ERIIGRNETI
     PTAKAQDFTT YKDGQTALAI HVVQGERDLV QDCRSLARFE LRGIPPMAAG AARIRVTFTV
     DADGLLSVAA REQASGVEAR IDVKPSYGLS DEQIARMLQE GFATAQQDMQ TRALVEARVD
     ADRLLIATQS ALDVDGDVLA AAERTAIDDL MHALRATLET STDAAAVEAA AQALAKGTEA
     FAAQRMNRGI RQALAGKNVS AL