ID E4T9F1_RIEAD Unreviewed; 635 AA.
AC E4T9F1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
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 ORFNames=RA0C_0686 {ECO:0000313|EMBL:AFD55646.1};
OS Riemerella anatipestifer (strain ATCC 11845 / DSM 15868 / JCM 9532 / NCTC
OS 11014).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=693978 {ECO:0000313|EMBL:AFD55646.1, ECO:0000313|Proteomes:UP000010093};
RN [1] {ECO:0000313|EMBL:AFD55646.1, ECO:0000313|Proteomes:UP000010093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15868 {ECO:0000313|Proteomes:UP000010093};
RX PubMed=22628503; DOI=10.1128/JB.00366-12;
RA Wang X., Zhu D., Wang M., Cheng A., Jia R., Zhou Y., Chen Z., Luo Q.,
RA Liu F., Wang Y., Chen X.Y.;
RT "Complete genome sequence of Riemerella anatipestifer reference strain.";
RL J. Bacteriol. 194:3270-3271(2012).
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; CP003388; AFD55646.1; -; Genomic_DNA.
DR RefSeq; WP_004920090.1; NC_017045.1.
DR AlphaFoldDB; E4T9F1; -.
DR GeneID; 66848143; -.
DR KEGG; rai:RA0C_0686; -.
DR KEGG; ran:Riean_0464; -.
DR PATRIC; fig|693978.17.peg.697; -.
DR HOGENOM; CLU_005965_2_1_10; -.
DR Proteomes; UP000010093; 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; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 605..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 635 AA; 68237 MW; 5AD313FB62E45EF2 CRC64;
MSKIIGIDLG TTNSCVAVME GKDPVVIPNA EGKRTTPSIV AFTEDGERKV GDPAKRQAVT
NPKNTVYSIK RFIGANFKTD ANEVSRVPYQ VVEGSNDTVK VKIGDREYTP QEISAMILQK
MKKTAEDYLG QEVSRAVITV PAYFNDAQRQ ATKEAGEIAG LKVERIINEP TAAALAYGLD
KVGKKDMNVV VFDCGGGTHD VSVLEMYEVD GNASFEVKAT DGDTHLGGDD FDNVIIDWMA
AEFQAEEGVD LKSDAIALQR LKEAAEKAKV ELSSSTQTEI NLPYITATAS GPKHLVKTLT
RAKFEQLAGD LIQRTIEPCK SALKNAGMSV SDIDEIILVG GSTRIPAIQE AVEKFFGKAP
SKGVNPDEVV AIGAAIQGGV LTGDVKDVLL LDVTPLSLGI ETMGSVFTKL IEANTTIPTK
KSEVFSTAVD NQPAVTIRVG QGERPMFNDN KEIGRFELTD IPPAPRGVPQ IEVTFDIDAN
GILSVSAKDK GTGKEQSIKI QASSGLSDEE IERMKREAEE NSAADAKKKE EADLINKADG
QIFQTEKQIK EFGDKISADK KSAIETALAE LKTAYEAKDM ANIKTKSEAL DAAWMAASEE
LYKAQAEAQG GAEQAQANTG NATDDVQDAD FEEVK
//
