ID A0A3S4V770_9ACTO Unreviewed; 630 AA.
AC A0A3S4V770;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chaperone protein DnaK {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:VEI13551.1};
GN ORFNames=NCTC13354_01268 {ECO:0000313|EMBL:VEI13551.1};
OS Trueperella bialowiezensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=312285 {ECO:0000313|EMBL:VEI13551.1, ECO:0000313|Proteomes:UP000269542};
RN [1] {ECO:0000313|EMBL:VEI13551.1, ECO:0000313|Proteomes:UP000269542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13354 {ECO:0000313|EMBL:VEI13551.1,
RC ECO:0000313|Proteomes:UP000269542};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LR134476; VEI13551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4V770; -.
DR KEGG; tbw:NCTC13354_01268; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000269542; Chromosome 1.
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; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 2.
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}; Chaperone {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:UP000269542};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 588..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 230..257
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 488..515
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 176
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 630 AA; 67841 MW; 1F93E03FFAB636FD CRC64;
MARAVGIDLG TTNSVVSVLE GGEPTVIANA EGQRTTPSVV GFSKTGEVLV GEIAKRQAVT
NVERTIQSVK RHMGDPNWKV EIDDKTYNAQ QISAFILQKL KKDAEAYLGE KVTDAVITVP
AYFNDAQRQA TKDAGQIAGL NVQRIVNEPT AAALAYGLEK GKEDELILVF DLGGGTFDVS
LLEVGKDDDD FSIIQVRATS GDNKLGGDDW DQRIVDWLVQ QVKNGYGVDL SKDKIALQRL
REAAEQAKKE LSSTTSTSIT LQYLSMSENG PIHLDETLTR AKFEEMTRDL LERTKAPFKK
VIEDAGIQLS EIDHVVMVGG STRMPAVTEV VKEMTGGREP NKGVNPDEVV AVGAALQAGV
ITGDRTDVLL IDVTPLSLGI ETKGGVMTKL IERNTAIPTK RSETFSTAED NQPSVLIQVY
QGERPFARDN KQLGTFELSG IAPAPRGVPQ IEVTFDIDAN GIVHVSAKDL GTGKEQSVTI
TGGSALSKED IERMVKEAEE NAAEDEKRRE AAEVRNTAEQ QVYSLEKLLD DNKDKLDDAV
VTEVREAVDA LKKALEGDDV EAIKSAQDDL NTKAQKIGEA LYADAQAQQS GEGWTEAAKA
AQESAAGAAG GADDDVVDAE IVDDEDQSKN
//
