ID E6TNQ8_MYCSR Unreviewed; 622 AA.
AC E6TNQ8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=Mspyr1_05160 {ECO:0000313|EMBL:ADT97225.1};
OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS (Mycobacterium gilvum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT97225.1, ECO:0000313|Proteomes:UP000008916};
RN [1] {ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADT97225.1, ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RX PubMed=22180818;
RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT reclassification to Mycobacterium gilvum Spyr1.";
RL Stand. Genomic Sci. 5:144-153(2011).
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; CP002385; ADT97225.1; -; Genomic_DNA.
DR RefSeq; WP_011891261.1; NC_014814.1.
DR AlphaFoldDB; E6TNQ8; -.
DR SMR; E6TNQ8; -.
DR KEGG; msp:Mspyr1_05160; -.
DR HOGENOM; CLU_005965_2_1_11; -.
DR Proteomes; UP000008916; 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 CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
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; 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}; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 494..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..251
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 494..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 622 AA; 66605 MW; 11DD7A375708CCCC CRC64;
MARAVGIDLG TTNSVVAVLE GGDPVVVANS EGSRTTPSVV AFARNGEVLV GQPAKNQAVT
NVDRTIRSVK REIGTDWSVE IDGKNYTPQE ISARVLMKLK RDAESYLGED ITDAVITVPA
YFNDAQRQAT KDAGQIAGLN VLRIVNEPTA AALAYGLDKG EKEQTILVFD LGGGTFDVSL
LEIGEGVVEV RATSGDNHLG GDDWDDRIVE WLVDKFKGTS GIDLTKDKMA MQRLREAAEK
AKIELSSSQS TSINLPYITV DADKNPLFLD EQLTRSEFQK ITQDLLDRTR KPFQSVIKDA
GISVGEIDHV VLVGGSTRMP AVSELVKEMT GGKEPNKGVN PDEVVAVGAA LQAGVLKGEV
KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTADDNQPSV QIQVFQGERE
IASHNKLLGS FELTGIPPAP RGVPQIEVTF DIDANGIVHV TAKDKGTGKE NTIKIQEGSG
LSKEEIDRMI KDAEAHADED RKRREEADVR NQAESLVYQT EKFVKEQREA EGGSKVPEDT
LTKVDAAISD AKAALAGTDI AAIKSAMEKL GEESQALGQA IYEATQAEQA AGGAPGGEST
GASNSGDDVV DAEVVEDDQE RK
//
