ID   A0A1H4GIG3_9BACT        Unreviewed;       637 AA.
AC   A0A1H4GIG3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05660909_05333 {ECO:0000313|EMBL:SEB08800.1};
OS   Chitinophaga terrae (ex Kim and Jung 2007).
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=408074 {ECO:0000313|EMBL:SEB08800.1, ECO:0000313|Proteomes:UP000199656};
RN   [1] {ECO:0000313|Proteomes:UP000199656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23920 {ECO:0000313|Proteomes:UP000199656};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNRL01000040; SEB08800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4GIG3; -.
DR   STRING; 408074.SAMN05660909_05333; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000199656; 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; 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   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          596..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   637 AA;  68910 MW;  D900E0A6772C9B5A CRC64;
     MGKIIGIDLG TTNSCVAVME GNEPVVIAND EGRRTTPSVV AFLKNGERKV GDPAKRQAIT
     NPVNTIMSVK RFMGRHFDEV ANEISHVTYK VVRGDNNTTR IDIDGRLYTP QEISAMILQK
     MKKTAEDYLG QEVNEAVITV PAYFNDAQRQ ATKEAGEIAG LNVRRIINEP TAAALAYGLD
     KKHADSKIAV FDLGGGTFDI SILELGDGVF EVKSTNGDTH LGGDDFDKVI MDWLADEFKK
     DEAVDLHKDP MAWQRLKEAA EKAKIELSSS QETEINLPYI TAVDGVPKHL VKKLTRAKFE
     QLSDSLVERT LEPCRKALKD AGLNTSEIDE IILVGGSTRI PKIQEVVEKF FGKKPNKGVN
     PDEVVAVGAA IQGGVLTGEV KDVLLLDVTP LSLGIETMGG VMTKLIEANT TIPTKKSETF
     STAADNQPSV EINVLQGERP MANQNRSLGR FILNDIPPAP RGVPKIEVTF DIDANGILHV
     TAKDQGTGKT QNIRIEAGSG LSKEEVEKMK AEAKANETAD KEQREKIETL NKADSLIFQT
     EKQVKEYGDK LPADKKAAIE SALNKLREAH KAQDVAQVNT AMPELEAAWT AASEELYKAS
     QGQPGGAEGA QANAGGAQGQ QGGGNDGVTD AEFEEVK
//