ID   HSCA_VIBVU              Reviewed;         617 AA.
AC   Q8DEZ1;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VV1_0434;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable chaperone. Has a low intrinsic ATPase activity which
CC       is markedly stimulated by HscB (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00679}.
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DR   EMBL; AE016795; AAO08957.1; -; Genomic_DNA.
DR   RefSeq; WP_011078533.1; NC_004459.3.
DR   AlphaFoldDB; Q8DEZ1; -.
DR   SMR; Q8DEZ1; -.
DR   EnsemblBacteria; AAO08957; AAO08957; VV1_0434.
DR   KEGG; vvu:VV1_0434; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000002275; Chromosome 1.
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..617
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078654"
SQ   SEQUENCE   617 AA;  66095 MW;  431A85D10E09BE87 CRC64;
     MALLQIAEPG QSSAPHEHKR AAGIDLGTTN SLVASVRSGT ADTLKDAQGR SLLPSIVNYA
     NEEAIVGYEA KALSESQPQD TIISVKRLLG RSLTDIQTRY PSLPYRFKAS ENGLPVLQTT
     QGDKNPIEVS ADILKVLAKR AEESLGGELS GVVITVPAYF DDAQRAGTKD AAKLAGLHVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SKGVFEVLAT GGDSALGGDD
     FDHLLADFLA EQAGLETPLS 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