DNAK_CHLFF
ID DNAK_CHLFF Reviewed; 664 AA.
AC Q253K1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=CF0765;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(2006).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; AP006861; BAE81537.1; -; Genomic_DNA.
DR RefSeq; WP_011458315.1; NC_007899.1.
DR AlphaFoldDB; Q253K1; -.
DR SMR; Q253K1; -.
DR STRING; 264202.CF0765; -.
DR KEGG; cfe:CF0765; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_0; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001260; 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 Stress response.
FT CHAIN 1..664
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000205177"
FT REGION 574..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 664 AA; 71622 MW; D1DC6BCE7D61DF0D CRC64;
MSEHKKSSKI IGIDLGTTNS CVSVMEGGQA KVITSSEGTR TTPSIVAFKG SETLVGIPAK
RQAVTNPEKT LASTKRFIGR KYSEVESEIK TVPYKVTSGS NGDAVFQVEG KQYTPEEIGA
HILMKMKETA EAYLGETITE AVITVPAYFN DSQRASTKDA GRIAGLDVKR IIPEPTAAAL
AYGIDKAGDK KIAVFDLGGG TFDISILEIG DGVFEVLSTN GDTHLGGDDF DEVIIKWMIE
EFQKQEGIDL GKDNMALQRL KDAAEKAKIE LSGMSSTEIN QPFITMDANG PKHLTLTLTR
AHFEKLASNL IERTKAPCIK ALADAKLSAS DIDDVLLVGG MSRMPAVQEI VKDIFGKEPN
KGVNPDEVVA IGAAIQGGVL GGEVKDVLLL DVIPLSLGIE TLGGVMTPLV ERNTTIPTQK
KQIFSTAADN QPAVTIVVLQ GERPMAKDNK EIGRFDLTDI PPAPRGHPQI EVTFDIDANG
ILHVSAKDAA SGREQKIRIE ASSGLKEDEI QRMIRDAEQN KEEDKKRREA SDVRNEADSM
IFRAEKAIND YKANIPESLV KEIEERVEKV RSALKEDAST EKIKEASEEL SRHMQKIGEA
MQSQSASAAP SSAANAQGGP NINTEDLKKH SFSTKPPAGN STSASSNNEN IEEADVEIVD
KPND