ID   HSCA_SHEB8              Reviewed;         620 AA.
AC   A6WNY1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN   OrderedLocusNames=Shew185_2382;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
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., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-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; CP000753; ABS08520.1; -; Genomic_DNA.
DR   RefSeq; WP_012089340.1; NC_009665.1.
DR   AlphaFoldDB; A6WNY1; -.
DR   SMR; A6WNY1; -.
DR   KEGG; sbm:Shew185_2382; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
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_1000044886"
SQ   SEQUENCE   620 AA;  66151 MW;  54E654F83518493C CRC64;
     MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGE TATLPDELGQ HSLPSIVRYT
     QDSVEVGALA ALSSAQDPQN TIVSVKRFMG RSLADIKAGE QSFPYEFAES ENGLPLFVTP
     QGQVNPVQVS AEILRPLIAR AEKTLGGELQ GVVITVPAYF DDAQRQGTKD AAALLGVKVL
     RLLNEPTAAA IAYGLDSKQE GVIAIYDLGG GTFDISILRL NRGVFEVLAT GGDSALGGDD
     FDHLLQAHMQ QVWQLSDIDS QLSRQLLIES RRVKEALTDA AETEAKVILA DGTELTQIVS
     KAEFDAMIAA LVKKTIASCR RTLRDAGVTT DEVLETVMVG GSTRVPLVRE QVEAFFGKPP
     LTSIDPDRVV AIGAAIQADI LVGNKPESDL LLLDVIPLSL GIETMGGLVE KVVSRNTTIP
     VARAQEFTTF KDGQTAMAFH VVQGERELVA DCRSLARFTL KGIPPLAAGA AHIRVTFQVD
     ADGLLSVTAM EKSTGVQSSI QVKPSFGLSD TEIATMLKDS MKYAKDDIGR RMLAEQQVEA
     ARVLESLHAA LAKDGDLLNA DERGQIDATM ANVAQVAAGD DADAIKLAIE KLDEQTQDFA
     ARRMDNSIRV AFKGQSIDNI