ID   HSCA_SHEPW              Reviewed;         620 AA.
AC   B8CMW9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=swp_1699;
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877;
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ28471.1; -; Genomic_DNA.
DR   RefSeq; WP_020911849.1; NC_011566.1.
DR   AlphaFoldDB; B8CMW9; -.
DR   SMR; B8CMW9; -.
DR   STRING; 225849.swp_1699; -.
DR   EnsemblBacteria; ACJ28471; ACJ28471; swp_1699.
DR   KEGG; swp:swp_1699; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000753; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131694"
SQ   SEQUENCE   620 AA;  65729 MW;  AE6F91B607A6E6BC CRC64;
     MALLQIAEPG LTAAPHQHRL AVGIDLGTTN SLVAAVRSGV ANTLADESAQ HSLPSVVRYT
     QDSVFVGREA EAFSAQDPQN TIISVKRFMG RSLDDIQSGS QTFPYIFEAS DNGLPIFITP
     QGKVNPIQVS ADILKPLVER AESTLGGTLE GVVITVPAYF DDAQRQGTKE AAALVGVKVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL NKGVFEVLAT GGDSALGGDD
     FDHMLQAHFQ QQWSLDEVSA GLSRMLLIEA RKVKEALTDS DNTTANVTDD NGNVLSLNVS
     RATFDEMISK LVKKTVSSCR RALRDAGVST DEVIETVMVG GSTRVPLVRG EVANFFGKTP
     LTSIDPDRVV AIGAAIQADI LVGNKPDSDL LLLDVIPLSL GIETMGGLVE KVVARNTTIP
     VARAQEFTTF KDGQTAMAFH VVQGERELVA DCRSLARFTL NGIPPLAAGA AHIRVTFQVD
     ADGLLSVTAM EKSTGVKTTI QVKPSFGLSD AEIGSMLKDS MANAKEDISR RMLAEKQVEA
     ARVLESLSAA LNKDGQLLAA NELSAIQGAM ALLAQLAEEK DTDAIEDAIE ALDTATQDFA
     AKRMDNSIKL ALKGQSVDNI