ID   HSCA_VIBVY              Reviewed;         617 AA.
AC   Q7MNF8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VV0759;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC93523.1; -; Genomic_DNA.
DR   RefSeq; WP_011149603.1; NC_005139.1.
DR   AlphaFoldDB; Q7MNF8; -.
DR   SMR; Q7MNF8; -.
DR   STRING; 672.VV93_v1c07050; -.
DR   PRIDE; Q7MNF8; -.
DR   EnsemblBacteria; BAC93523; BAC93523; BAC93523.
DR   KEGG; vvy:VV0759; -.
DR   PATRIC; fig|196600.6.peg.774; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002675; 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..617
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078655"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  66065 MW;  4421723EF2585C21 CRC64;
     MALLQIAEPG QSSAPHEHKR AAGIDLGTTN SLVASVRSGT ADTLKDAQGR SLLPSIVNYA
     NEEAIVGYAA KALSESQPQD TIISVKRLLG RSLTDIQTRY PSLPYRFKAS ENGLPVLQTT
     QGDKNPIEVS ADILKVLAKR AEESLGGELS GVVITVPAYF DDAQRAGTKD AAKLAGLHVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SKGVFEVLAT GGDSALGGDD
     FDHLLADFLA EQVGLETPLS AEKNRTLLNI ATATKIAFSE QDSVEVEVFG WKGVVTREQF
     EELIRPLVKK TLMSCRRALK DADVEADEVL EVVMVGGSTR TLLVREMVGE FFGRTPLTNI
     NPDEVVAIGA GIQADILAGN KPDSEMLLLD VIPLSLGIET MGGLVEKIIP RNTTIPVARA
     QEFTTFKDGQ TAMSVHIVQG EREMVDDCRS LARFSLKGIP PMAAGAAHIR VTYQVDADGL
     LSVTAMEKST GVQSEIQVKP SYGLSDDEVA NMLRDSMTYA KEDMQARALA EQRVEADRVI
     EGLIAAMQAD GDELLSEAEK ATLLQAIESL IELRNGNEAN AIEQGIKDTD KASQDFASRR
     MDKSIRAALA GQSIDTI