ID U5Q7V1_9BACT Unreviewed; 660 AA.
AC U5Q7V1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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:AGY53430.1};
GN ORFNames=BRDCF_p803 {ECO:0000313|EMBL:AGY53430.1};
OS Bacteroidales bacterium CF.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY53430.1, ECO:0000313|Proteomes:UP000017642};
RN [1] {ECO:0000313|EMBL:AGY53430.1, ECO:0000313|Proteomes:UP000017642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AGY53430.1};
RX PubMed=24356833;
RA Tang S., Edwards E.A.;
RT "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT Dechlorinating Enrichment Culture.";
RL Genome Announc. 1:e01066-13(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; CP006772; AGY53430.1; -; Genomic_DNA.
DR AlphaFoldDB; U5Q7V1; -.
DR STRING; 1400053.BRDCF_p803; -.
DR KEGG; bacc:BRDCF_p803; -.
DR HOGENOM; CLU_005965_2_1_10; -.
DR Proteomes; UP000017642; 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 CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
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; 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 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:UP000017642};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 609..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 660 AA; 71421 MW; 82EBAE64BBCE8654 CRC64;
MFDTYRANTN RNKQKLTDIM GKIIGIDLGT TNSCVAVMEG NEPTVIINSE GKRTTPSVVA
FADNGERKIG DPAKRQAITN PTKTIYSIKR FMGESFDRVQ TEVGRVPYKV DRGDNNTSRV
NIDGRLYTPQ EISAMVLQKM KKTAEDYLGQ EVTEAVITVP AYFSDSQRQA TKEAGEIAGL
KVKRIINEPT AAALAYGLDK MHRDMKVAVF DLGGGTFDIS ILELGEGVFE VKSTNGDTHL
GGDDFDQKII DWLADEFKSE NSGIDLRKDP MALQRLKEAA EKAKIELSSQ TASEINLPYI
MPVDGVPKHL VKTLTRAKFE QICDTLIQKT VEPCRKALSD ANYKPSDIDE VLLVGGSTRI
PAIQQIVEKF FGKAPSKGVN PDEVVAVGAA IQGGVLAGDV KDVLLLDVTP LSLGIETYGS
VMTKLIESNT TIPTRKSEVF STASDNQPSV EIHVLQGERP MAKDNKTIGR FHLDGIAPAP
RGVPQIEVTF DIDANGILNV SAKDKGTGKE QKIRIEASSG LSESEIKRMR DEAKANEAAD
KAEREKVDKI NAADGMIFQT EKNLKEYGDK IPSDKKGAIE SALATLKEAH KSGDVAAIDK
AMESMNAAWH AASEDMAKAA QSGPSQSAGS DQGQSNDNGG NSSSNGGDKE VTDVDFEEVK
//
