ID A0A1Y4N8T1_9FIRM Unreviewed; 621 AA.
AC A0A1Y4N8T1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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=B5F08_08870 {ECO:0000313|EMBL:OUP77288.1};
OS Anaeromassilibacillus sp. An172.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaeromassilibacillus.
OX NCBI_TaxID=1965570 {ECO:0000313|EMBL:OUP77288.1, ECO:0000313|Proteomes:UP000195869};
RN [1] {ECO:0000313|Proteomes:UP000195869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An172 {ECO:0000313|Proteomes:UP000195869};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC 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:OUP77288.1}.
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DR EMBL; NFKS01000018; OUP77288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4N8T1; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000195869; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000195869};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 571..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 621 AA; 66243 MW; 9835B76BCF1AA8AE CRC64;
MAKTIGIDLG TTNSCVAVIE GGEPVVIPNA EGSRTTPSVV AFKGGERLVG QVAKRQAITN
PNTVSSIKRE MGSDYKVNIE GKSYTPQEIS AMILQKLKAD AEAYLGEKVT QAVITVPAYF
TDAQRQATKD AGKIAGLDVK RIINEPTAAA LSYGIDKEKD QKVMVYDLGG GTFDVSIIEM
GDGVQEVLAT AGNNRLGGDD FDQRIINWMI QGFKSETGID LSGDKMAMQR LKEAAEKAKI
DLSGITTASI NLPFITADAT GPKHLDMTLT RAKFNELTSD LVESTMGPVR RALSDSGLQI
GEIDKVLMVG GSSRIPAVQE AVKNFIGKEP FKGINPDECV AVGAAIQGGV LGGEVEGLLL
LDVTPLSLGV ETMGGVMTKV IDRNTTIPTK KSQIFSTAAD NQTQVEINVL QGEREFARDN
KQLGLFTLSG IAPAMRGVPQ IEVTFDIDAN GIVNVSAKDL GTGKEQKITI SSSTNMSKDD
IDKAVREAEQ YAAEDKKRRE EVDAKNEAEN MAYQAEKLVN ESGDKMDAAD KEALKTKAAA
VKDAIAKNDK TMIDAAKEDL QKKLYEVSSK MYQQAAPQQN PQGAPDMGNM GGNPYGQAPN
GGAQPNGNVY DADFTDVDGQ N
//
