ID   HSCA_SHESM              Reviewed;         620 AA.
AC   Q0HJF0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN   OrderedLocusNames=Shewmr4_1743;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-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; CP000446; ABI38817.1; -; Genomic_DNA.
DR   RefSeq; WP_011622514.1; NC_008321.1.
DR   AlphaFoldDB; Q0HJF0; -.
DR   SMR; Q0HJF0; -.
DR   KEGG; she:Shewmr4_1743; -.
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_1000044892"
SQ   SEQUENCE   620 AA;  66409 MW;  5C2EE2E575010E1B CRC64;
     MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGV TATLPDENGQ HSLPSIVRYT
     QDGIEVGQVA ALSSAQDPKN TIVSVKRFMG RSLTDIQSGE QAFPYQFEAS ENGLPLFVTP
     QGQVNPVQVS AEILRPLVER AEKTLGGELQ GVVITVPAYF DDAQRQGTKD AASLLGVKVL
     RLLNEPTAAA IAYGLDSKQE GVIAIYDLGG GTFDISILRL NRGVFEVLAT GGDSALGGDD
     FDHLLQAHMQ QVWQLTNLDP QLSRQLLIEA RRVKEALTDA SDVEASLTLA DGTVLKQVVT
     KAEFDNLISA LVKKTIASCR RTLRDAGVTA DEVLETVMVG GSTRVPLVRE QVEAFFGKAP
     LTSIDPDRVV AIGAAIQADI LVGNKPESEL LLLDVIPLSL GIETMGGLVE KVVSRNTTIP
     VARAQEFTTF KDGQTAMAFH VVQGERELVD DCRSLARFTL KGIPPLAAGA AHIRVTFQVD
     ADGLLSVTAM EKSTGVQSSI QVKPSFGLSD TEIATMLKDS MKHAKEDISR RMLAEQQVEA
     ARVLESLNAA LAKDGDLLTS DERQQIDAVM AQLAEIARGD DADAIKQAIE VLDEHTQDFA
     AKRMDNSIRV AFKGQSIDNI