ID M9WA28_9MOLU Unreviewed; 593 AA.
AC M9WA28;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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 ECO:0000313|EMBL:AGJ90853.1};
GN ORFNames=MPUT9231_4430 {ECO:0000313|EMBL:AGJ90853.1};
OS Mycoplasma putrefaciens Mput9231.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1292033 {ECO:0000313|EMBL:AGJ90853.1, ECO:0000313|Proteomes:UP000012984};
RN [1] {ECO:0000313|EMBL:AGJ90853.1, ECO:0000313|Proteomes:UP000012984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mput9231 {ECO:0000313|EMBL:AGJ90853.1};
RX PubMed=23766410;
RA Dupuy V., Sirand-Pugnet P., Baranowski E., Barre A., Breton M., Couture C.,
RA Dordet-Frisoni E., Gaurivaud P., Jacob D., Lemaitre C., Manso-Silvan L.,
RA Nikolski M., Nouvel L.X., Poumarat F., Tardy F., Thebault P., Theil S.,
RA Citti C., Blanchard A., Thiaucourt F.;
RT "Complete Genome Sequence of Mycoplasma putrefaciens Strain 9231, One of
RT the Agents of Contagious Agalactia in Goats.";
RL Genome Announc. 1:e00354-13(2013).
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; CP004357; AGJ90853.1; -; Genomic_DNA.
DR RefSeq; WP_015587445.1; NC_021083.1.
DR AlphaFoldDB; M9WA28; -.
DR KEGG; mput:MPUT9231_4430; -.
DR PATRIC; fig|1292033.3.peg.431; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_14; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000012984; 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; 3.30.420.40; -; 2.
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; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000012984};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 572..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..251
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 579..593
FT /note="Polar 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 593 AA; 64457 MW; 301F9BCFAA6C1A6B CRC64;
MSKEKIIGID LGTTNSVVSV IEGGQPVILE NPEGQRTTPS VVAFKNSDII VGGAAKRQAV
TNPNVVQSIK SKMGTTQKVN LENKDYTPEQ ISAEILRYMK NYAESKLGQK ISKAVITVPA
YFNDAQRKAT KDAGKIAGLE VERIINEPTA AALAYGLDKA NKEEKVLVYD LGGGTFDVSI
LEIADGTFEV LSTSGNNKLG GDNFDEAVIN WLLEKIKAEF AIDLSQDKMA RQRLKDEAEK
AKINLSSQLE VEINLPFIAM NDNGPISFAT TLSRSEFNKI TKHLVDLTSQ PVQDALREAK
LTSKDIDEVL LVGGSTRIPA VQDLVKSLLK KEPNRSINPD EVVAMGAAIQ GAVLAGDVKD
VLLLDVTPLS LGIETMGGIM TKLIERNTTI PTEKSQIFST AADNQPAVDI NILQGERPMA
ADNKSLGQFQ LTGIQPAPKG VPQIEVTFKI DANGIVSVSA KDKQTNEEKS ITISNSGNLS
DDEINRMVKE AEENAASDEI KKKNVELKNK AESYVNVIET SIKEAGDKVT PEQKEQSEKM
LSEIKELIKN EDYAGLEQKM SELEQAMAAA AEFAKQQGFD PNQDPNQDPN QQQ
//
