DNAK_STRM5
ID DNAK_STRM5 Reviewed; 641 AA.
AC B4SSQ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Smal_1600;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF51305.1; -; Genomic_DNA.
DR RefSeq; WP_012510757.1; NC_011071.1.
DR AlphaFoldDB; B4SSQ6; -.
DR SMR; B4SSQ6; -.
DR STRING; 391008.Smal_1600; -.
DR PRIDE; B4SSQ6; -.
DR EnsemblBacteria; ACF51305; ACF51305; Smal_1600.
DR KEGG; smt:Smal_1600; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; SMAL391008:SMAL_RS08235-MON; -.
DR Proteomes; UP000001867; 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; 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 Stress response.
FT CHAIN 1..641
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119760"
FT REGION 604..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 641 AA; 68668 MW; 354A212620480F19 CRC64;
MGKIIGIDLG TTNSCVAIMD GGKARVIENS EGDRTTPSIV AYTKDGEVLV GASAKRQAVT
NPKNTFYAVK RLIGRKFTDA EVQKDIAHVP YSILAHDNGD AWVATSDAKK MAPQEISAKV
LEKMKKTAED FLGEKVTEAV ITVPAYFNDS QRQATKDAGR IAGLDVKRII NEPTAAALAY
GLDKGDNKDR KIVVYDLGGG TFDVSVIEIA NVDGEKQFEV LATNGDTFLG GEDFDNRVIE
YLVEEFNKDQ GIDLRKDPLA LQRLKDAAER AKIELSSAQQ TEVNLPYVTA DASGPKHLNI
KLTRAKLESL VEELIRKSIE PCRVALNDAG LRSSDISEVI LVGGQTRMPK VQQAVTEFFG
KEPRKDVNPD EAVALGAAIQ GGVLGGDVKD VLLLDVTPLS LGIETMGGVF TKIIEKNTTI
PTKASQVFST AEDNQSAVTV HVLQGEREQA RFNKSLAKFD LSGIEPAPRG LPQVEVSFDI
DANGILHVSA KDKKTNKEQK VEIKAGSGLS EEEIARMVAD AEANREEDKK FQELVQARNQ
ADALIHGTRS AITEHGSKVG GDVIGKVEAA LADLETAMKG DDKAQIEAKS KVLEEAGQSL
FAAASAEQGG AAPGADAGNA GKAQDDVVDA EFTEVKDDKK S