ID   HSCA_SHESR              Reviewed;         620 AA.
AC   Q0HVP0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN   OrderedLocusNames=Shewmr7_1823;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
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 chromosome 1 of Shewanella sp. MR-7.";
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; CP000444; ABI42815.1; -; Genomic_DNA.
DR   RefSeq; WP_011626053.1; NC_008322.1.
DR   AlphaFoldDB; Q0HVP0; -.
DR   SMR; Q0HVP0; -.
DR   EnsemblBacteria; ABI42815; ABI42815; Shewmr7_1823.
DR   KEGG; shm:Shewmr7_1823; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
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_1000044893"
SQ   SEQUENCE   620 AA;  66465 MW;  717E3259B46BCCBA CRC64;
     MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGV TATLPDENGQ HSLPSIVRYT
     QDGIEVGQVA ALSSAQDPKN TIVSVKRFMG RSLTDIQSGE QIFPYQFEAS ENGLPLFVTP
     QGQVNPVQVS AEILRPLVER AEKTLGGELQ GVVITVPAYF DDAQRQGTKD AASLLGVKVL
     RLLNEPTAAA IAYGLDSKQE GVIAIYDLGG GTFDISILRL NRGVFEVLAT GGDSALGGDD
     FDHLLQAHMQ QVWQLTNLDP QLSRQLLIEA RRVKEALTDA SEVEASLTLA 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 AKLAEIARGD DADAIKQAIE VLDEHTQDFA
     AKRMDNSIRV AFKGQSIDNI