ID U5DLT3_9CHRO Unreviewed; 639 AA.
AC U5DLT3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=KR51_00015170 {ECO:0000313|EMBL:ERN41852.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN41852.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN41852.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN41852.1,
RC ECO:0000313|Proteomes:UP000016960};
RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERN41852.1}.
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DR EMBL; ASSJ01000040; ERN41852.1; -; Genomic_DNA.
DR RefSeq; WP_022606184.1; NZ_ASSJ01000040.1.
DR AlphaFoldDB; U5DLT3; -.
DR STRING; 582515.KR51_00015170; -.
DR PATRIC; fig|582515.4.peg.1714; -.
DR eggNOG; COG0443; Bacteria.
DR InParanoid; U5DLT3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000016960; Unassembled WGS sequence.
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; 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:UP000016960};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 486..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..274
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 486..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..533
FT /note="Basic and acidic 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 639 AA; 68405 MW; 703AA9416A98D354 CRC64;
MAKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AYAKNGDRLV GQIAKRQAVM
NPGNTFYSVK RFIGRKHEEV SNESTEVAYN VLRDGSGNVK IDCPAASKQF APEEISAQVL
RKLVEDASKY LGEQVTQAVI TVPAYFNDSQ RQATKDAGKI AGIEVLRIIN EPTAASLAYG
MEKKSNETIL VFDLGGGTFD VSILEVGDGV FEVLATSGDT HLGGDDFDKK IVDYLAGEFK
QAEGIDLRQD KQALQRLTEA AEKAKIELSS VTQADVNLPF ITATQDGPKH LDTTLTRAKF
EDLCSDLIDR CRIPVESSLR DAKLGKGDID EIVLVGGSTR IPAIKDLVKR VLDKDPHQGV
NPDEVVAVGA AVQAGVLGGE VKDILLLDVT PLSLGVETLG GVMTTMIPRN TTIPTKKAET
FSTAVDGQTN VEIHVLQGER EFAKDNKDLG IFRLDGIPPA PRGVPQIEVT FDIDANGILN
VTAKDKGTGK EQSISITGAS TLSDDEVNRM VDEAEKNASE DKERRERIER KNQADSLVYQ
ADKQLQELGD KVPADDKSKA EGLIADLRDA VAKEDDDRIQ TLMPELQQTL YSIGTNVYQQ
GAPAGAPDGS APDSGPTDAG SSASSDGDDV IDAEFSETK
//
