ID V3R301_9ENTR Unreviewed; 637 AA.
AC V3R301;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415, ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332};
GN ORFNames=L370_02008 {ECO:0000313|EMBL:ESN15944.1};
OS Enterobacter sp. MGH 24.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=1329828 {ECO:0000313|EMBL:ESN15944.1, ECO:0000313|Proteomes:UP000017624};
RN [1] {ECO:0000313|EMBL:ESN15944.1, ECO:0000313|Proteomes:UP000017624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGH 24 {ECO:0000313|EMBL:ESN15944.1,
RC ECO:0000313|Proteomes:UP000017624};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Murphy C., Cosimi L., Cerqueira G., Feldgarden M., Hung D., Onderdonk A.B.,
RA Ferraro M.J., Hooper D., Dekker J., O'Brien T., Huang S., Quan V.,
RA Ernst C., Delaney M., DuBois A., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterobacter cloacae complex MGH 24.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESN15944.1}.
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DR EMBL; AYJG01000003; ESN15944.1; -; Genomic_DNA.
DR RefSeq; WP_023310346.1; NZ_KI535657.1.
DR AlphaFoldDB; V3R301; -.
DR GeneID; 63140786; -.
DR PATRIC; fig|1329828.3.peg.1960; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR Proteomes; UP000017624; Unassembled WGS sequence.
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; 3.30.420.40; -; 2.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375:SF541; CHAPERONE PROTEIN DNAK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00332};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00332};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 599..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 637 AA; 69032 MW; B246C0FD5FECD5CF CRC64;
MGKIIGIDLG TTNSCVAIMD GTTARVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT
NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP YKIIAADNGD AWLDVKGTKT APPQISAEVL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKEVGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDTRLINYL
VDEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIQDVILV GGQTRMPMVQ KKVAEFFGKE
PRKDVNPDEA VAIGAAVQGG VLTGEVKDVL LLDVTPLSLG IETMGGVMTA LINKNTTIPT
KHSQVFSTAE DNQSAVTIHV IQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA
DGILHVSAKD KNSGKEQKIT IKASSGLNEA EIEKMVRDAE ANAESDRKFE ELVQTRNQGD
HLLHSTRKQV EEAGDKLPAE DKTAIEAALS ALESSLKGED KADIEAKMQE LAQASQKLME
IAQQQHAQQQ AGADASANNA KDDDVVDAEF EEVKDKK
//
