ID   HSCA_VEREI              Reviewed;         622 AA.
AC   A1WKG6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Veis_2377;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
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 Verminephrobacter eiseniae EF01-2.";
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; CP000542; ABM58123.1; -; Genomic_DNA.
DR   RefSeq; WP_011810126.1; NC_008786.1.
DR   AlphaFoldDB; A1WKG6; -.
DR   SMR; A1WKG6; -.
DR   STRING; 391735.Veis_2377; -.
DR   EnsemblBacteria; ABM58123; ABM58123; Veis_2377.
DR   KEGG; vei:Veis_2377; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000374; 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_1000044900"
SQ   SEQUENCE   622 AA;  65716 MW;  C46AB52DC05D4695 CRC64;
     MALLQISEPG QSPHPHQRRI AVGIDLGTTH SLVAAVRNGV SECLPDAQGR VLLPSVVRYL
     DQGGRQIGHE AVAAQVWDAR NTIASVKRFM GRSLKDVARA GQLPYDFVPD AAAQGMLSLA
     TVAGNKSPVE VSAEILAALR QRAEDSFNAD LYGAVITVPA YFDDAQRQAT KDAARLAGIP
     LLRLINEPTA AAIAYGLDNA SEGIYAVYDL GGGTFDISIL RLAQGVFEVI ATGGDSALGG
     DDYDAALVDW VLQQARRQAS TPADRAALRI AARACKQALS ATDIAAFSAD ISCANVHVDV
     RRADFEAITA DLTARSMAAV RRALRDAQLT RDQVQGVVLV GGATRMPQVQ RAVAQFFGQP
     PLTNLNPDEV VALGAAIQAH QLAGNGGNAA ELLLLDVIPL SLGVETMGGL VERIVARNEP
     IPTAKAQDFT TYKDGQTALA IHVVQGERDL VQDCRSLARF ELRGIPPMVA GAARIRVTFA
     IDADGLLSVS AKEQGSGAQA HIDVKPSYGL SDEQIARMLQ DSFATAAQDM KTRALVEARV
     DAERMLSATQ SALAADGEML SARERAAIEA LMATLSAQRE ADDAAVIEAA TEALAQGTQA
     FAARRMNRGI RQALAGRNVQ TL