ID G2DFY2_9GAMM Unreviewed; 652 AA.
AC G2DFY2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:EGV50462.1};
GN ORFNames=Rifp1Sym_da00050 {ECO:0000313|EMBL:EGV50462.1};
OS endosymbiont of Riftia pachyptila (vent Ph05).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1048808 {ECO:0000313|EMBL:EGV50462.1, ECO:0000313|Proteomes:UP000004491};
RN [1] {ECO:0000313|EMBL:EGV50462.1, ECO:0000313|Proteomes:UP000004491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(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}.
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:EGV50462.1}.
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DR EMBL; AFOC01000080; EGV50462.1; -; Genomic_DNA.
DR RefSeq; WP_005965151.1; NZ_AFOC01000080.1.
DR AlphaFoldDB; G2DFY2; -.
DR PATRIC; fig|1048808.3.peg.2556; -.
DR Proteomes; UP000004491; 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 608..652
FT /note="Disordered"
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 652 AA; 69847 MW; F632DBA5238696FF CRC64;
MGKIIGIDLG TTNSCVAVME GDTTKVIENS EGDRTTPSII AYANDGEILV GQSAKRQAVT
NPHHTLFAIK RLIGRMFQDK VVQRDVDMVP YKIVKADNGD AWVEVNGKKM APPEISAKIL
QKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
MDKKRGDQTL AVYDLGGGTF DISIIEIAEI DGEHQFEVLS TNGDTFLGGE DFDMRIIDFL
VEEFKKEQGF DLRNDPLALQ RLKEAAEKAK VELSGSQQTD INLPYITADQ TGPKHLNIKL
TRAKLEALVD DLVTRTIEPC KVALKDAGIS TSDIDEVILV GGQSRMPKVQ EQVQAFFGKE
PRRDVNPDEA VAIGAAIQGG VLGGDVKDVL LLDVTPLSLG IETLGGVMTK LIEKNTTIPT
SASQTFSTAD DNQTAVTVHV LQGEREQAAA NKSLGRFDLT DIPPAPRGMP QIEVSFDIDA
NGILNVSAKD KATGKEQSIV IKASSGLSDD EVERMVKDAE AHAEEDKQFQ ELAGSRNQAD
NMIHAVKKAM DDLGDEKMEG NEKETIEAAI KDLEAVIKGD DKAAIEAKTK ALTDASGKMM
ERLYAQQSGE AGAAAGAAAG AGAADAGADA GSQAGGDDVV DAEFEEVKDD KK
//
