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Database: UniProt
Entry: Q87PR2_VIBPA
LinkDB: Q87PR2_VIBPA
Original site: Q87PR2_VIBPA 
ID   Q87PR2_VIBPA            Unreviewed;       647 AA.
AC   Q87PR2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=DnaK-related protein {ECO:0000313|EMBL:BAC59702.1};
GN   OrderedLocusNames=VP1439 {ECO:0000313|EMBL:BAC59702.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59702.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC59702.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
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   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; BA000031; BAC59702.1; -; Genomic_DNA.
DR   RefSeq; NP_797818.1; NC_004603.1.
DR   AlphaFoldDB; Q87PR2; -.
DR   KEGG; vpa:VP1439; -.
DR   PATRIC; fig|223926.6.peg.1375; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_030332_0_0_6; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10170; HSP70_NBD; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002493}.
SQ   SEQUENCE   647 AA;  70366 MW;  842D7334F2FE40AA CRC64;
     MNQENLSQET AQEQQSPKFS VGIDLGTTHC VMSYVDTQDE DARVQVMPIP QLTAPGTVET
     RSQLGSFLYQ PHEHEMNPQS RVLPWSSEPK ALVGAIARNL GSKTPIRLVA SAKSWLCHAG
     VNRRDAFLPT GSPEEVEKVS PLRATELYLE HLKDAWNHAN PNHKLADQDV TITVPASFDP
     AARDLTAEAA RNVGFVHLTL LEEPQAALYN WIDNSNDKWR DEVEVGDIVL VVDIGGGTTD
     LSLVEVTEDE GNLTLNRIAV GEHILLGGDN MDLALAYRLK MKLAQEGKEL QPWQVQAMTH
     ACRDAKEALL NDSALQSVPI VVPSRGSKLL GATLKTELTQ EEVQQTLVDG FFPQVAITDH
     PVQRNRGALT QMGLPYAQDA GITRHIAAFL SKQAHAQSGG ESAQAQDFNP FANMPGMPGS
     DAAQSADFIK PTAILFNGGV LKSKLLATRL EDTINKWLIE ADAEMAKRLT GVDLDLAVAS
     GAAYYGSVRR GQGVRIRGGI ASAYYVGIES AMPAIPGMAP PMEALCVAPF GMEEGSSVDV
     PSQEFGLIIG QPVNFQFFGS TVRRDDLAGT HLDYWAPEEL EELPEIQVTL PVSEGRREGE
     VVPVTLASRV TELGTLYLEA IAADNGQKWH VEFDVREDAK SDSNEEQ
//
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