ID   HSCA_ALIFM              Reviewed;         616 AA.
AC   B5FAW4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VFMJ11_0635;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP001139; ACH66849.1; -; Genomic_DNA.
DR   RefSeq; WP_012534025.1; NC_011184.1.
DR   AlphaFoldDB; B5FAW4; -.
DR   SMR; B5FAW4; -.
DR   EnsemblBacteria; ACH66849; ACH66849; VFMJ11_0635.
DR   KEGG; vfm:VFMJ11_0635; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001857; Chromosome I.
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..616
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131697"
SQ   SEQUENCE   616 AA;  65945 MW;  7275F84AE8BD0B4D CRC64;
     MLLQIAEPGQ SAVPHQHKLA VGIDLGTTNS LVASVRSGEA KTLPDMKGNV ILPSVVQYQE
     DKICVGMNAY QSAAMDPQNT IISVKRLMGR SLKDIQARYP ELPYQFSESE NGLPVIQTAQ
     GEVNPIQVSS EILKSLSRRA QDTLGGELEG VVITVPAYFD DAQRAGTKDA ATLAGLNVLR
     LLNEPTAAAI AYGLDSGQEG VIAVYDLGGG TFDISILRLS KGVFEVLATG GDSALGGDDF
     DHVLAQWIKE QAGITSSLSS QEQRELLTLA TQTKVALSDS DNVKISFKDW SGEISVELFN
     SLIQPLIKKT LMACRRALKD ADITSEEVME VVMVGGSTRT PFVRTSVGDY FGQTPLTSID
     PDQVVAIGAA IQADILVGNK PDSEMLLLDV IPLSLGIETM GGLVEKIIPR NTTIPVAKAQ
     EFTTFKDGQT GMMVHVVQGE REMVEDGRSL ARFSLKGIPP MAAGAAHIRV TYQVDADGLL
     SVTAMEKSTG VQSHIQVKPS YGLSDNEVAN MLKDSMTYAK EDMQARALAE QQVEADRVIE
     GLVVALNNDG DALLSKEEQA EILQAIEALI TLRQGTDAQA IEDGIKKADE ASQEFAARRM
     DASIRAALAG QSIDEV