ID A0A2P8VH34_9ENTR Unreviewed; 638 AA.
AC A0A2P8VH34;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=C7G83_14630 {ECO:0000313|EMBL:PSN06834.1};
OS Siccibacter turicensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Siccibacter.
OX NCBI_TaxID=357233 {ECO:0000313|EMBL:PSN06834.1, ECO:0000313|Proteomes:UP000240212};
RN [1] {ECO:0000313|EMBL:PSN06834.1, ECO:0000313|Proteomes:UP000240212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6100069499-17 {ECO:0000313|EMBL:PSN06834.1,
RC ECO:0000313|Proteomes:UP000240212};
RA Lepuschitz S., Pekard-Amenitsch S., Haunold R., Schill S., Mach R.,
RA Allerberger F., Ruppitsch W., Forsythe S.J.;
RT "Draft genome sequence of the first documented clinical Siccibacter
RT turicensis isolate in Austria.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:PSN06834.1}.
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DR EMBL; PYEP01000006; PSN06834.1; -; Genomic_DNA.
DR RefSeq; WP_024550232.1; NZ_RYYT01000006.1.
DR AlphaFoldDB; A0A2P8VH34; -.
DR STRING; 1388748.GCA_000463155_00532; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000240212; 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 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 602..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..617
FT /note="Polar 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 638 AA; 69252 MW; 85AAD829CD8B7D16 CRC64;
MGKIIGIDLG TTNSCVAIMD GTTARVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT
NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP YKIIGADNGD AWLDVKGQKM APPQISAEVL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
LDKEVGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRMINYL
VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIQDVILV GGQTRMPMVQ KKVAEFFGKE
PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTP LITKNTTIPT
KHSQVFSTAE DNQSAVTIHV LQGERKRASD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA
DGILHVSAKD KNSGKEQKIT IKASSGLNEE EIQKMVQEAE ANAESDRKFE ELVQTRNQGD
HLLHSTRKQV EEAGEQLPAD DKTAIESALS ALETSLKGED KADIEAKMQA LAQVSQKLME
IAQQQHAQQQ AGSADASANN AKEDDVVDAE FEEVKDKK
//
