ID A0A0W0TT91_9GAMM Unreviewed; 644 AA.
AC A0A0W0TT91;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ECO:0000313|EMBL:KTC98852.1};
GN ORFNames=E4T54_08370 {ECO:0000313|EMBL:QBS12757.1}, Lgee_1429
GN {ECO:0000313|EMBL:KTC98852.1};
OS Legionella geestiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45065 {ECO:0000313|EMBL:KTC98852.1, ECO:0000313|Proteomes:UP000054785};
RN [1] {ECO:0000313|EMBL:KTC98852.1, ECO:0000313|Proteomes:UP000054785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTC98852.1,
RC ECO:0000313|Proteomes:UP000054785};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBS12757.1, ECO:0000313|Proteomes:UP000294523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1308 {ECO:0000313|EMBL:QBS12757.1,
RC ECO:0000313|Proteomes:UP000294523};
RA Durieux I., Ginevra C., Attaiech L., Picq K., Juan P.A., Jarraud S.,
RA Charpentier X.;
RT "Diverse conjugative elements silence natural transformation in Legionella
RT species.";
RL Submitted (MAR-2019) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNYC01000055; KTC98852.1; -; Genomic_DNA.
DR EMBL; CP038271; QBS12757.1; -; Genomic_DNA.
DR RefSeq; WP_028387497.1; NZ_UGNZ01000001.1.
DR AlphaFoldDB; A0A0W0TT91; -.
DR STRING; 45065.Lgee_1429; -.
DR KEGG; lgt:E4T54_08370; -.
DR PATRIC; fig|45065.4.peg.1546; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000054785; Unassembled WGS sequence.
DR Proteomes; UP000294523; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000054785};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 606..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 536..563
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 644 AA; 68843 MW; 6BF0997C47D9BF98 CRC64;
MAKIIGIDLG TTNSCVAVLE GDTRKVIENS EGARTTPSIV AYTDDGEVLV GQAAKRQAVT
NPKNTLFAIK RLIGRKFKDP IVQKDIKMVP YEIVSADNGD AWVRVKGDDK APPQISAEVL
RKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
MDKKRGDSVI AVYDLGGGTF DISIIEIAEV DGEHQFEVLA TNGDTFLGGE DFDLALIEYL
SAEFKKDTGI DLHNDPLALQ RLKEAAEKAK IELSSAQQTD VNLPYITADA SGPKHMNIKL
TRAKLESLVE GLVQRSIAPC KTALKDAGKS VSEIDEVILV GGQTRMPLVQ KTVQDLFGKE
PRKDVNPDEA VAVGAAIQAG VLSGDVKDIL LLDVTPLSLG IETLGGVMTK LIEKNTTIPT
KANQVFSTAD DNQTAVTVHV LQGEREQASA NKSLGRFDLS DIPPAPRGMP QIEVTFDIDA
NGILNVSAKD KATGKAQSIV IKASSGLSDE EIDAMVKDAK AHADEDRKFR EMADLRNQAD
GLIHSSEKSL KDLEAEMDAD EKSAIENAIA ALKEAVKGTD KAELEAKIKT LSDASGKMAE
RVYAKKAGSG SEAAGGEAAG AQTASSDDGV VDAEFEEVRD DEKK
//
