ID A0A222P4T5_9GAMM Unreviewed; 645 AA.
AC A0A222P4T5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:ASQ46870.1};
GN ORFNames=clem_11665 {ECO:0000313|EMBL:ASQ46870.1};
OS Legionella clemsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1867846 {ECO:0000313|EMBL:ASQ46870.1, ECO:0000313|Proteomes:UP000201728};
RN [1] {ECO:0000313|Proteomes:UP000201728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC-D5610 {ECO:0000313|Proteomes:UP000201728};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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}.
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DR EMBL; CP016397; ASQ46870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222P4T5; -.
DR KEGG; lcd:clem_11665; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000201728; 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 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:UP000201728};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 605..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..645
FT /note="Basic and acidic 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 645 AA; 69976 MW; 7FDF2C40AAAAAD93 CRC64;
MAKIIGIDLG TTNSCVAIME GNQPRVIENS EGHRTTPSIV AYTDDNEILV GAAAKRQAVT
NPDNTVFAVK RLIGRRFDDP IVQKDIKMVP YKIIKADNGD AWVQVKGQDK APPQISAEVL
RKMKKTAEDY LGEEVKEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
MDKKRGDSVI AVYDLGGGTF DISIIEIAEV DGEHQFEVLA TNGDTFLGGE DFDLALIEYL
AAEFKKDSGI DLHSDPLALQ RLKDAAEKAK IELSSAQQTD VNLPYITADA SGPKHLNIKL
TRAKLESLVE HLVERSIEPC KIALKDAGLK VSQINEVILV GGQTRMPMVQ KKVQEFFGKE
PRKDVNPDEA VAVGAAIQAA VLSGDVKDIL LLDVTPLSLG IETLGGVMTK LIEKNTTIPT
KANQVFSTAD DNQTAVTVHV LQGEREQASA NKSLGRFDLT DIPPAPRGVP QIEVIFDIDA
NGILNVSAKD KATGKAQSIV IKASSGLSEE EVEAMIKDAK SHADEDKKFK EMAEIRNQAD
ALIHSSEKSM KDLEGELSAD EKTSIESAIA ELKEAIKGND KVQIEEKLKV LTNVSGKMAE
RVYAKKTAET QSQQPSDEAK PSEEAKQADE GVVDAEFEEV QDDKK
//
