ID U5NG49_9MOLU Unreviewed; 614 AA.
AC U5NG49;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 46.
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:AGX89169.1};
GN ORFNames=PRV_02155 {ECO:0000313|EMBL:AGX89169.1};
OS Mycoplasma parvum str. Indiana.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1403316 {ECO:0000313|EMBL:AGX89169.1, ECO:0000313|Proteomes:UP000017119};
RN [1] {ECO:0000313|EMBL:AGX89169.1, ECO:0000313|Proteomes:UP000017119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indiana {ECO:0000313|EMBL:AGX89169.1,
RC ECO:0000313|Proteomes:UP000017119};
RX PubMed=24285648;
RA do Nascimento N.C., Dos Santos A.P., Chu Y., Guimaraes A.M., Pagliaro A.,
RA Messick J.B.;
RT "Genome Sequence of Mycoplasma parvum (Formerly Eperythrozoon parvum), a
RT Diminutive Hemoplasma of the Pig.";
RL Genome Announc. 1:e00986-13(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; CP006771; AGX89169.1; -; Genomic_DNA.
DR RefSeq; WP_022770072.1; NC_022575.1.
DR AlphaFoldDB; U5NG49; -.
DR STRING; 1403316.PRV_02155; -.
DR KEGG; mpv:PRV_02155; -.
DR PATRIC; fig|1403316.3.peg.400; -.
DR HOGENOM; CLU_005965_2_4_14; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000017119; 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; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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:UP000017119};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 570..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 483..510
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 578..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 614 AA; 67874 MW; C9DE32EDC1D9F9C1 CRC64;
MAVKKEIILG IDLGTTNSCV AIVEGGNPKV LETPEGKRTV PSVVSFKGDQ IIVGDSAKRQ
MVTNKNTIFS IKRFIGTDKK VVAQGKEYSP EEISAYILSY IKEYAEKRVG EKVQKAVITV
PAYFNDSQRQ STKNAGKIAG LEVVRIVNEP TAAALAYGLD KKDKEQKILV YDLGGGTFDV
SVLEVSDGTF QVLSTSGDNN LGGDDWDQRI IRWMLESIQK EHGVDLSKDN LVMQRLKEAA
EKAKIELSSV QQTQIMLPFL TMVKGEPLNI DLSLTREQFQ LFTKDLLERT VDPVKDAIKE
SKLSLSEINE VLLVGGSTRM PAVQELVEKL TNKKPNLSIN PDEVVALGAS VQAGILAGDI
KDILLLDVTP LTLSIETLGG VATPLIPRNS TIPIDKKQLF STAVDNQPSV DIHVVQGERP
MASQNKSLGT FTLHGIKQAP KGMPKIEVSF SIDANGILTV KAEDKDTGKQ SNITINQASG
LSEDEINKII KEAEENLEKD KKVREEIEIK NEAESWVSML EKQISDDSAK LPEESKKEAQ
KVVDEFKKLI EEKKYDELKS KMEELKNLSQ KMMQEAYKQH QDSGKTEEQF EAESPEANAK
EVEVEDISSE ENNK
//
