DNAK2_COLP3
ID DNAK2_COLP3 Reviewed; 638 AA.
AC Q47XI6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Chaperone protein DnaK 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein 2 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 2 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK2 {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=CPS_3821;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP000083; AAZ27124.1; -; Genomic_DNA.
DR RefSeq; WP_011044570.1; NC_003910.7.
DR AlphaFoldDB; Q47XI6; -.
DR SMR; Q47XI6; -.
DR STRING; 167879.CPS_3821; -.
DR EnsemblBacteria; AAZ27124; AAZ27124; CPS_3821.
DR KEGG; cps:CPS_3821; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; DKMVLQR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000547; Chromosome.
DR GO; GO:0005524; F:ATP binding; 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 Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
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; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..638
FT /note="Chaperone protein DnaK 2"
FT /id="PRO_0000225952"
FT REGION 604..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 638 AA; 68766 MW; FA89096B20160DBA CRC64;
MGKIIGIDLG TTNSCVAVLD GDSVRVIENA EGDRTTPSII GYTAEGETLV GQPAKRQSVT
NPENTLYAIK RLIGRRFEDK ETQRDIDIMP FGIVKADNGD AWVQVKGEKI APPQVSAEVL
KKMKKTAEDF LGETVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
MDKQEGDKVV AVYDLGGGTF DISIIEIDEM DGEHTFEVLA TNGDTHLGGE DFDNRLINYL
VAEFKKDQGM DLTSDPLAMQ RLKEAAEKAK CELSSAQQTD VNLPYITADG SGPKHMNIKV
TRAKLESLVE DMVKATLEPL KQALKDADLS VSKIDDVILV GGQSRMPLVQ KTVTDFFGKE
PRKDVNPDEA VASGAAIQAG VLSGDVTDVL LLDVTPLSLG IETMGGVMTK VIDKNTTIPT
KQSQTFSTAD DNQAAVTVHV CQGERKQASA NKSLGQFNLE GIEPAQRGTP QIEVTFDIDA
DGILHVTAKD KNTGKEQKIT IKASSGLSDE EVEQMVRDAE ANADADAKFE ELVTARNQAD
GMIHATRKQV EEAGEELPSE DKEKIEAALT ELEEAVKGDD KEVIEAKTQA LMEASAKLME
IAQAKEQAQS APEGAQEADA APADDVVDAE FEEVKDDK