DNAK_CHLTR
ID DNAK_CHLTR Reviewed; 660 AA.
AC P17821; O84401; P16896; Q46400;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=75 kDa membrane protein;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=CT_396;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L2;
RX PubMed=2365454; DOI=10.1128/iai.58.7.2098-2104.1990;
RA Birkelund S., Lundemose A.G., Christiansen G.;
RT "The 75-kilodalton cytoplasmic Chlamydia trachomatis L2 polypeptide is a
RT DnaK-like protein.";
RL Infect. Immun. 58:2098-2104(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=2294048; DOI=10.1128/iai.58.1.189-196.1990;
RA Danilition S.L., Maclean I.W., Peeling R., Winston S., Brunham R.C.;
RT "The 75-kilodalton protein of Chlamydia trachomatis: a member of the heat
RT shock protein 70 family?";
RL Infect. Immun. 58:189-196(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-626.
RC STRAIN=E/UW-5/Cx;
RX PubMed=8226832; DOI=10.1016/s0021-9258(19)49438-6;
RA Raulston J.E., Davis C.H., Schmiel D.H., Morgan M.M., Wyrick P.B.;
RT "Molecular characterization and outer membrane association of a Chlamydia
RT trachomatis protein related to the hsp70 family of proteins.";
RL J. Biol. Chem. 268:23139-23147(1993).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Expressed early during infection.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; X52175; CAA36423.1; -; Genomic_DNA.
DR EMBL; M27580; AAA03644.1; -; Unassigned_DNA.
DR EMBL; AE001273; AAC67993.1; -; Genomic_DNA.
DR EMBL; L22180; AAC36839.1; -; Unassigned_DNA.
DR PIR; A40158; A40158.
DR PIR; B71521; B71521.
DR RefSeq; NP_219906.1; NC_000117.1.
DR RefSeq; WP_009871748.1; NC_000117.1.
DR AlphaFoldDB; P17821; -.
DR SMR; P17821; -.
DR STRING; 813.O172_02155; -.
DR EnsemblBacteria; AAC67993; AAC67993; CT_396.
DR GeneID; 884718; -.
DR KEGG; ctr:CT_396; -.
DR PATRIC; fig|272561.5.peg.426; -.
DR HOGENOM; CLU_005965_2_1_0; -.
DR InParanoid; P17821; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000431; 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; 2.60.34.10; -; 1.
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 PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..660
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078446"
FT REGION 608..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT VARIANT 593
FT /note="H -> R (in strain: L2 and E/UW-5/Cx)"
FT CONFLICT 194..211
FT /note="VFDLGGGTFDISILEIGD -> SLRLRRRNFRYFYLGNRWI (in Ref.
FT 2; AAA03644)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..240
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 353..362
FT /note="EIFGKEPNKG -> RSLVKSLIKA (in Ref. 2; AAA03644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 70824 MW; 438900096477FF11 CRC64;
MSEKRKSNKI IGIDLGTTNS CVSVMEGGQP KVIASSEGTR TTPSIVAFKG GETLVGIPAK
RQAVTNPEKT LASTKRFIGR KFSEVESEIK TVPYKVAPNS KGDAVFDVEQ KLYTPEEIGA
QILMKMKETA EAYLGETVTE AVITVPAYFN DSQRASTKDA GRIAGLDVKR IIPEPTAAAL
AYGIDKEGDK KIAVFDLGGG TFDISILEIG DGVFEVLSTN GDTHLGGDDF DGVIINWMLD
EFKKQEGIDL SKDNMALQRL KDAAEKAKIE LSGVSSTEIN QPFITIDANG PKHLALTLTR
AQFEHLASSL IERTKQPCAQ ALKDAKLSAS DIDDVLLVGG MSRMPAVQAV VKEIFGKEPN
KGVNPDEVVA IGAAIQGGVL GGEVKDVLLL DVIPLSLGIE TLGGVMTPLV ERNTTIPTQK
KQIFSTAADN QPAVTIVVLQ GERPMAKDNK EIGRFDLTDI PPAPRGHPQI EVTFDIDANG
ILHVSAKDAA SGREQKIRIE ASSGLKEDEI QQMIRDAELH KEEDKQRKEA SDVKNEADGM
IFRAEKAVKD YHDKIPAELV KEIEEHIEKV RQAIKEDAST TAIKAASDEL STHMQKIGEA
MQAQSASAAA SSAANAQGGP NINSEDLKKH SFSTRPPAGG SASSTDNIED ADVEIVDKPE
