ID   HSCA_SHEPA              Reviewed;         620 AA.
AC   A8H2N0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Spea_1492;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) 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; CP000851; ABV86817.1; -; Genomic_DNA.
DR   RefSeq; WP_012154743.1; NC_009901.1.
DR   AlphaFoldDB; A8H2N0; -.
DR   SMR; A8H2N0; -.
DR   STRING; 398579.Spea_1492; -.
DR   PRIDE; A8H2N0; -.
DR   EnsemblBacteria; ABV86817; ABV86817; Spea_1492.
DR   KEGG; spl:Spea_1492; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000002608; 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; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000082989"
SQ   SEQUENCE   620 AA;  65952 MW;  CCCE45290B6B928D CRC64;
     MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGV ANTLPDEDSQ HSLPSVVRYT
     QDSVLVGREA EAFSAQDPQN TIVSIKRFMG RSLEDIQSGD QTLPYIFEAS ENGLPIFVTP
     SGKVNPVQIS SEILKPLVAR AELTLGGTLE GVVITVPAYF DDAQRQGTKD AASLTGVKVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL NKGVFEVLAT GGDSALGGDD
     FDHMLQAYFA EQWQVSSASA SMNRKMQIEA RRVKEALTES AETTASVVDD AGTKLTLTVT
     RELFDSLIAK LVKKTISSCR RALRDAGVSN DEVLETVMVG GSTRVPLVRQ EVESFMGKTP
     LTSIDPDRVV AIGAAIQADI LVGNKPESDL LLLDVIPLSL GIETMGGLVE KVVSRNTTIP
     VARAQEFTTF KDGQTAMAFH VVQGERELVA DCRSLARFTL KGIPPLAAGA AHIRVTFQVD
     ADGLLSVTAM EKSTGVQASI QVKPSFGLSD EEIGSMLKDS MANAKEDITR RMLAEKQVEA
     ARVLESLNAA LSKDSDLLSV DERGVIEANM ASLAQIASED DADAIEAAIE VLDTATQDFA
     AKRMDNSIRL ALKGQSVDNI