ID A0A090AK28_9ENTR Unreviewed; 640 AA.
AC A0A090AK28;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415, 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:BAP58793.1};
GN ORFNames=TGUWTKB_5670 {ECO:0000313|EMBL:BAP58793.1};
OS Candidatus Tachikawaea gelatinosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Tachikawaea.
OX NCBI_TaxID=1410383 {ECO:0000313|EMBL:BAP58793.1, ECO:0000313|Proteomes:UP000031627};
RN [1] {ECO:0000313|Proteomes:UP000031627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UwTKB {ECO:0000313|Proteomes:UP000031627};
RA Kaiwa N., Hosokawa T., Nikoh N., Meng X.Y., Tanahashi M., Moriyama M.,
RA Maeda T., Yamaguchi K., Shigenobu S., Ito M., Fukatsu T.;
RT "Symbiont-containing voluminous jelly as an extraordinary maternal gift for
RT overwintering insect nymphs.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAP58793.1, ECO:0000313|Proteomes:UP000031627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UwTKB {ECO:0000313|EMBL:BAP58793.1,
RC ECO:0000313|Proteomes:UP000031627};
RA Kaiwa N., Hosokawa T., Nikoh N., Tanahashi M., Moriyama M., Meng X.Y.,
RA Maeda T., Yamaguchi K., Shigenobu S., Ito M., Fukatsu T.;
RT "Symbiont-Supplemented Maternal Investment Underpinning Host's Ecological
RT Adaptation.";
RL Curr. Biol. 20:2465-2470(2014).
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; AP014521; BAP58793.1; -; Genomic_DNA.
DR RefSeq; WP_041063365.1; NZ_AP014521.1.
DR AlphaFoldDB; A0A090AK28; -.
DR STRING; 1410383.TGUWTKB_5670; -.
DR KEGG; sbw:TGUWTKB_5670; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000031627; 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:SF541; CHAPERONE PROTEIN DNAK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, 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:UP000031627};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 605..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 640 AA; 70321 MW; D02855E562FC9C29 CRC64;
MGKIIGIDLG TTNSCVAVMD GKKARVLENA EGDRTTPSII AYTKDGETLV GQPAKRQAVT
NPKNTLFAIK RLIGRRFEDE EVQRDIKIMP YKIIKSDNGD AWLNIDNQKI APPQISAEVL
KKMKKTAEDY LGESVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAASLAYG
LDKSKGNQTI AVYDLGGGTF DISIIEIDDV DGEKTFEVLA TNGDTHLGGE DFDIRLINYL
VSEFKKDQGI NLQNDPLAMQ RLKESAEKAK IELSAAQQTD VNLPYITADS SGPKHLNIKV
TRAKLESLVE DLILRSIEPL KVALKDSKLS INNINDVILV GGQTRMPMVQ KKVAEFFGKE
PRKDVNPDEA VAVGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTA LINKNTTIPT
KHSQIFSTAE DNQSAVTIHV LQGERKRALD NKSLGQFNLD GIQSAPRGIP QIEVTFDIDA
DGILHVSAKD KNSGKEQKIT IKASSGLKEE EIKKMVQDAE INAEEDRKFE ELIRTKNQGD
QIIHNTNKQL KKVGDQLSVD DKKSIESSLD ALNLALKSED KNEIEDKIQK LLQVSGKLME
LIQKQEKDNA NNNTNTKNNS DKKNDDVVDA EFEEVKDNKK
//
