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DNAK_MYCAP
ID   DNAK_MYCAP              Reviewed;         598 AA.
AC   A5IXT5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=MAG1460;
OS   Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS   agalactiae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=347257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX   PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA   Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA   Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA   Blanchard A., Citti C.;
RT   "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT   bacterial genome.";
RL   PLoS Genet. 3:744-758(2007).
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; CU179680; CAL58844.1; -; Genomic_DNA.
DR   RefSeq; WP_011949326.1; NC_009497.1.
DR   AlphaFoldDB; A5IXT5; -.
DR   SMR; A5IXT5; -.
DR   STRING; 347257.MAG1460; -.
DR   PRIDE; A5IXT5; -.
DR   EnsemblBacteria; CAL58844; CAL58844; MAG1460.
DR   KEGG; maa:MAG1460; -.
DR   HOGENOM; CLU_005965_2_4_14; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000007065; 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; 2.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
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   CHAIN           1..598
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119733"
FT   REGION          571..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   598 AA;  65246 MW;  216D371EAD4230CA CRC64;
     MAKEVIIGID LGTTNSVVSI VDNGSPVVLE NLNGKRTTPS VVSFKDGEII VGDNAKNQIE
     TNPDTVASIK RLMGTSKTVH VNNKDYKPEE ISAMILEHLK KYAEEKIGHK VEKAVITVPA
     YFDNAQREAT KIAGKIAGLE VLRIINEPTA AALAFGLDKV KKEQKILVFD LGGGTFDVSI
     LELAEGTFEV LSTAGDNRLG GDDWDNEIVK WLIDLIKKDY KTDVTNNKMA MARLKAAAEK
     AKIDLSSSQQ ATIMLPFLVM QQGSEPISVE ATLRRSQFEE MTSHLVERCR KPIETALADA
     KIKISDLDDV ILVGGSTRIP AVQQLVESIL NKKANRSVNP DEVVAMGAAI QGAVLAGEID
     DVLLVDVTPL TLGIETAGGI ATPLIPRNTR IPITKSEVFT TFEDNQSEVT IRIVQGERPL
     ASENKLLGQF NLGGIRVAPR GVPQIEVSFK IDANGITTVL AKDKDTNKEQ SITIKNSSKL
     SESEIEEMIK DAEKNREADA KRAEEISTII QAENLVNSLE KEMNDGNIVI PEEEKAKIAD
     YIKEVKELIN NKDVEQLKKK IDELNAAYNM AKSAAASSNK DDSLNNNSSS NNDEETFE
 
 
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