ID   A0A944GF74_9DELT        Unreviewed;       629 AA.
AC   A0A944GF74;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   24-JUL-2024, entry version 5.
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   ECO:0000313|EMBL:MBS7381446.1};
GN   ORFNames=KIG72_09285 {ECO:0000313|EMBL:MBS7381446.1};
OS   Bradymonadales bacterium.
OC   Bacteria; Deltaproteobacteria; Bradymonadales.
OX   NCBI_TaxID=2099667 {ECO:0000313|EMBL:MBS7381446.1, ECO:0000313|Proteomes:UP000748917};
RN   [1] {ECO:0000313|EMBL:MBS7381446.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=164 {ECO:0000313|EMBL:MBS7381446.1};
RA   Crossfield M.G., Gilroy R.;
RT   "Recovery of novel microbial genomes from metagenomic faecal samples of
RT   pigs.";
RL   Submitted (MAY-2021) 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:MBS7381446.1}.
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DR   EMBL; JAHAXN010000516; MBS7381446.1; -; Genomic_DNA.
DR   Proteomes; UP000748917; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          598..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          245..272
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         196
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   629 AA;  68352 MW;  5AE443A3B01A1FEE CRC64;
     MAKIIGIDLG TTNSCVAVLE GTEPKVITNE EGDRTTPSVV AFDDKGETIV GQFARRQATM
     NYENTIFSAK RFIGMKYSER IDEAKHMPFK VIQMSNGSAG FEVRGKQFTP PEISAKVLQK
     LKRDAEKYLG QQVTEAVITV PAYFNDSQRQ ATKDAGKIAG LNVRRIINEP TAAALAYGLD
     KKKDETIAVY DFGGGTFDIS ILEVGDNVVE VISTNGDTHL GGDNIDELII DWLVKEFKKD
     SGIDVSNDKM VLQRLRDEAE KAKKALSTMT STDINLPFLT ADATGPKHLN VNLSRAKFED
     MIADVVQKTL EPCKKALRDA NKSVSDIDEV VLVGGSTRIP LVQQEVEKFF GKKSNHSVNP
     DEVVALGAAI QGGVLAGDVK DILLLDVTPL SLGIETLGGV TTKLIPRNTT IPTRKSEIFT
     TADDNQTKVT VHVLQGEREM AAQNRTLAKF NLEGIPAAPR GVPQIEVTFD INADGIVNVS
     AKDKATGKEQ RVTIEASSGL NQSDIDRMVN DAKEHEAEDK KRREVVDAKN ELESLIFSAE
     KSIKDYGDKL QASDVEALQK AIEEAKTKKD SEDIDTLKAA KDALMAASHK IAEVMYAQAN
     NQGTQQPGAA PGAAGKKDDD VIDAEFEEN
//