ID F9YRV3_CAPCC Unreviewed; 630 AA.
AC F9YRV3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 OrderedLocusNames=Ccan_16380 {ECO:0000313|EMBL:AEK23754.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23754.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK23754.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
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; CP002113; AEK23754.1; -; Genomic_DNA.
DR RefSeq; WP_013997740.1; NC_015846.1.
DR AlphaFoldDB; F9YRV3; -.
DR SMR; F9YRV3; -.
DR STRING; 860228.Ccan_16380; -.
DR KEGG; ccm:Ccan_16380; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_10; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000008895; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:AEK23754.1};
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:UP000008895};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 586..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 630 AA; 68540 MW; 2F728D6E1C34BD46 CRC64;
MSKIIGIDLG TTNSCVSVME GNDPVVITNA EGKRTTPSVV AFVDGGEIKV GDAAKRQAVT
NPKKTVYSIK RFMGNKFSES EKEVARVPYK VVKGDNDTPR VDIDGRLYTP QEISAMILQK
MKKTAEDFLG QTVTEAVITV PAYFNDAQRQ ATKEAGEIAG LKVRRIINEP TAAALAYGLD
KKHNDQKIVV FDFGGGTHDV SILELGDGVF EVLATDGDTH LGGDDVDEKI INWLAEEFQA
EEQMDLRKDP MALQRLKEAA EKAKIELSSS TQTEINLPYI TATATGPKHL VRTLTRAKFE
QLIDDLVKRT IEPCRTALKN AGLSTSDIDE VILVGGSTRI PAVQEAVEKF FGKKPNKSVN
PDEVVAVGAA IQGGVLTGDV KDVLLLDVTP LSLGIETMGG VMTKLIEANT TIPTKKSQVF
STAADNQPSV EIHVLQGERP MANDNKTIGR FHLDGIPPAP RGVPQIEVTF DIDANGIIKV
SATDKGTGKS HDIRIEASSG LSQEEIEKMK REAEANAEAD KKAKEKADKI NEADSMIFQT
EKQLKEFGDK LPADKKSGIE SALEELKKAH QSQDLGQIQP ALDRINEAWK QASEDLYKAQ
QAQSEPQPNT GGQQQQNGDN VQDVDFEEVR
//
