ID   HSCA_ALIF1              Reviewed;         616 AA.
AC   Q5E780;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VF_0621;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85116.1; -; Genomic_DNA.
DR   RefSeq; WP_011261362.1; NC_006840.2.
DR   RefSeq; YP_204004.1; NC_006840.2.
DR   AlphaFoldDB; Q5E780; -.
DR   SMR; Q5E780; -.
DR   STRING; 312309.VF_0621; -.
DR   EnsemblBacteria; AAW85116; AAW85116; VF_0621.
DR   KEGG; vfi:VF_0621; -.
DR   PATRIC; fig|312309.11.peg.613; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000537; 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; Reference proteome.
FT   CHAIN           1..616
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078652"
SQ   SEQUENCE   616 AA;  65955 MW;  AF6484F776EE074D 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 QAGITSPLSS 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 EDMKARALAE QQVEADRVIE
     GLVVALNNDG DALLSKEEQA EILQAIEALI TLRQGTDAQA IEDGIKKADE ASQEFAARRM
     DASIRAALAG QSIDEV