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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //