DNAK_PSYA2
ID DNAK_PSYA2 Reviewed; 647 AA.
AC Q4FPS9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Psyc_2132;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19979.1; -; Genomic_DNA.
DR RefSeq; WP_011281385.1; NC_007204.1.
DR AlphaFoldDB; Q4FPS9; -.
DR SMR; Q4FPS9; -.
DR STRING; 259536.Psyc_2132; -.
DR EnsemblBacteria; AAZ19979; AAZ19979; Psyc_2132.
DR KEGG; par:Psyc_2132; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000546; 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..647
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000226000"
FT REGION 605..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 647 AA; 69538 MW; 7A30B4E34053A7E7 CRC64;
MGKVIGIDLG TTNSCVAVME GDKVKIIENA EGTRTTPSIV AYKDDEILVG QSAKRQAVTN
PNNTLFAIKR LIGRRFDDKV VQKDIGMVPY KIAKADNGDA WVEINGKKLA PPQVSAEILK
KMKKTAEDYL GEAVTEAVVT VPAYFNDSQR QATKDAGKIA GLDVKRIINE PTAAALAYGM
DKKQGDSTVA VYDLGGGTFD VSIIEIADVD GEQQFEVLAT NGDTFLGGED FDSALIDFLV
AEFKKDQDVN LKGDSLAMQR LKEAAEKAKI ELSSAQSTEV NLPYITADSS GPKHLVVTIS
RSKLESLTEE LVQRTMGPCK MALEDAGIKI GDIDDVILVG GQTRMPLVQQ KVQEFFGQEP
RKDVNPDEAV AAGAAIQGAV LSGEKTDVLL LDVTPLTLGI ETMGGILTPI IEKNTMIPTK
KSQVFSTAED NQPAVSIQVY QGERKIANQN KQLGRFDLTD IPPAPRGLPQ IEVSFDINAD
GIMNISATDK GTGKAQSIQI KADSGLSDEE VEQMIRDAEA NAAEDEKFAN LAQVRNEADG
RIHAVQKALK DAADKVSDDE KSSVETAISE LEAAAKEDDH DDIKAKLEAL DNAFLPVSQK
IYADAGAGSE GMDPNQFQQG ADNAGENNQA DDDVVDAEFT EVEDDKK