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DNAK_CHLAB
ID   DNAK_CHLAB              Reviewed;         659 AA.
AC   Q8GH79; Q5L6M8;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 102.
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=CAB237;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AB7;
RX   PubMed=12056482; DOI=10.1051/vetres:2002019;
RA   Hechard C., Grepinet O., Rodolakis A.;
RT   "Protection evaluation against Chlamydophila abortus challenge by DNA
RT   vaccination with a dnaK-encoding plasmid in pregnant and non-pregnant
RT   mice.";
RL   Vet. Res. 33:313-326(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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; AF384685; AAN77259.1; -; Genomic_DNA.
DR   EMBL; CR848038; CAH63693.1; -; Genomic_DNA.
DR   RefSeq; WP_011096923.1; NC_004552.2.
DR   AlphaFoldDB; Q8GH79; -.
DR   SMR; Q8GH79; -.
DR   EnsemblBacteria; CAH63693; CAH63693; CAB237.
DR   KEGG; cab:CAB237; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001012; 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..659
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078441"
FT   REGION          571..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..595
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..646
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"
FT   CONFLICT        328
FT                   /note="A -> S (in Ref. 1; AAN77259)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   659 AA;  71104 MW;  D42167EFEDF60089 CRC64;
     MSEQKKSSKI IGIDLGTTNS CVSVMEGGQA KVIVSSEGTR TTPSIVAFKG NETLVGIPAK
     RQAVTNPAKT LASTKRFIGR KYSEVESEIK TVPYQVASGS NGDVVFPIDG KQFTPEEIGA
     QVLIKMKETA EAYLGEPVTE AVITVPAYFN DSQRASTKDA GRIAGLDVKR IIPEPTAAAL
     AYGIDKAGDK KIAVFDLGGG TFDISILEIG DGVFEVLSTN GDTHLGGDDF DEVIIKWMIE
     EFQKQEGIDL SKDNMALQRL KDAAEKAKIE LSGMSSTEIN QPFITMDANG PKHLTLTLTR
     AHFEKLASNL IERTKAPCQK ALADAKLAAS DIDDVLLVGG MSRMPAVQEV VKSIFGKEPN
     KGVNPDEVVA IGAAIQGGVL GGEVKDVLLL DVIPLSLGIE TLGGVMTPLV ERNTTIPTQK
     KQIFSTAADN QPAVTIVVLQ GERPMAKDNK EIGRFDLTDI PPAPRGHPQI EVTFDIDANG
     ILHVSAKDAA SGREQKIRIE ASSGLKEDEI QRMINDAEKN KEEDKKRREA SDVRNEADSM
     IFRAEKAISD YKENIPESLT KEIEERIEKV RSALKEDAPT EKIKEASDEL SRHMQKIGEA
     MQSQSASAAA NAQDGPNINT EDLKKHSFST KPPTGNSSSS ANNENIEEAD VEIVDKPND
 
 
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