ID   HSCA_VIBPA              Reviewed;         617 AA.
AC   Q87S24;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=VP0600;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC58863.1; -; Genomic_DNA.
DR   RefSeq; NP_796979.1; NC_004603.1.
DR   RefSeq; WP_005460220.1; NC_004603.1.
DR   AlphaFoldDB; Q87S24; -.
DR   SMR; Q87S24; -.
DR   STRING; 223926.28805586; -.
DR   PRIDE; Q87S24; -.
DR   EnsemblBacteria; BAC58863; BAC58863; BAC58863.
DR   GeneID; 1188075; -.
DR   KEGG; vpa:VP0600; -.
DR   PATRIC; fig|223926.6.peg.569; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000002493; 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; Reference proteome.
FT   CHAIN           1..617
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078653"
SQ   SEQUENCE   617 AA;  66095 MW;  43C1AA4CBD925EAD CRC64;
     MALLQIAEPG QSSAPHEHKL AAGIDLGTTN SLVASVRSGD ATTLNDEQGR SILPSVVNYS
     AESTVVGYDA KAKAEFEPEN TIISVKRLIG RSLKDIQSRY PSLPYRFKES DNGLPVLQTA
     QGDKNPIEVS ADILKALGKR AEETLGGDLA GVVITVPAYF DDAQRAGTKD AAKLAGLHVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SKGVFEVLAT GGDSALGGDD
     FDHLLADYLM EQAGLEAPLS AEKNRALLNI ATATKIAFSE QDSVEVDVFG WKGTVTREQF
     EDLIRPLVKK TLMSCRRALK DADVEAEEVL EVVMVGGSTR TLLVREMVGE FFGRTPLTSI
     NPDEVVAIGA GIQADILAGN KPDSEMLLLD VIPLSLGIET MGGLVEKIIP RNTTIPVARA
     QEFTTFKDGQ TAMSVHVVQG EREMVDDCRS LARFSLKGIP PMAAGAAHIR VTYQVDADGL
     LSVTAMEKST GVQSEIQVKP SYGLSDNEVA NMLRDSMTHA KEDMQARALA EQRVEADRVI
     EGLIAAMQAD GDELLSEQEK QDLLKAIEAL IELRNGDDAN AIEQGIKDTD KASQDFASRR
     MDKSIRAALS GQSVDDI