ID   HSCA_SHEHH              Reviewed;         620 AA.
AC   B0TNY5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Shal_1576;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000931; ABZ76142.1; -; Genomic_DNA.
DR   RefSeq; WP_012276681.1; NC_010334.1.
DR   AlphaFoldDB; B0TNY5; -.
DR   SMR; B0TNY5; -.
DR   STRING; 458817.Shal_1576; -.
DR   EnsemblBacteria; ABZ76142; ABZ76142; Shal_1576.
DR   KEGG; shl:Shal_1576; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001317; 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_1000082988"
SQ   SEQUENCE   620 AA;  66010 MW;  6A557E45F2A255E3 CRC64;
     MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGV ANTLPDEDSQ HSLPSVVRYT
     QSGVFVGREA EAFSAQDPQN TIVSVKRFMG RSLEDIQSGE QSLPYVFEAS ENGLPIFVTP
     NGKVNPVQIS SEILKPLVAR AESTLGGTLE GVVITVPAYF DDAQRQGTKD AASLTGVKVL
     RLLNEPTAAA IAYGLDSGQE GIIAVYDLGG GTFDISILRL NKGVFEVLAT GGDSALGGDD
     FDHMLQAHFA EQWQQGAVSA SMIRKMQIEA RRVKEALTES SETLATVIDD NGTELTLTVS
     RVLFEGLISK LVKKTISSCR RALRDAGVSS DEVLETVMVG GSTRVPLVRQ EVENFMGKVP
     LTSIDPDRVV AIGAAIQADI LVGNKPESDL LLLDVIPLSL GIETMGGLVE KVVSRNTTIP
     VARAQEFTTF KDGQTAMAFH VVQGERELVA DCRSLARFTL QGIPPLAAGA AHIRVTFQVD
     ADGLLSVTAM EKSTGVQSSI QVKPSFGLSD AEIGNMLKDS MANAKEDITR RMLAEKQVEA
     ARVLESLNAA LNKDADLLSE DEQSVIQTNM ASLAQIASED DADAIEAAIE VLDTATQDFA
     AKRMDNSIRL ALKGQSVDNI