ID A0A085LAX3_9FIRM Unreviewed; 614 AA.
AC A0A085LAX3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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:KFD42119.1};
GN ORFNames=DK28_0214360 {ECO:0000313|EMBL:KFD42119.1};
OS Peptococcaceae bacterium SCADC1_2_3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1487582 {ECO:0000313|EMBL:KFD42119.1, ECO:0000313|Proteomes:UP000027084};
RN [1] {ECO:0000313|EMBL:KFD42119.1, ECO:0000313|Proteomes:UP000027084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD42119.1};
RA Tan B.F., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFD42119.1, ECO:0000313|Proteomes:UP000027084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD42119.1};
RA Tan B., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RT "Draft genome sequence of an unculturable Firmicutes affiliated with
RT Peptococcaceae sorted using a microfluidic device from methanogenic alkane-
RT degrading cultures.";
RL Submitted (JUL-2014) 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:KFD42119.1}.
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DR EMBL; JJNX02000008; KFD42119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085LAX3; -.
DR STRING; 1487582.HY00_02275; -.
DR Proteomes; UP000027084; 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.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000027084};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 574..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 480..507
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 574..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 614 AA; 66911 MW; BAFC1C055F69A91F CRC64;
MAKVIGIDLG TTNSCMAVME GGEAVVIPNA EGGRTTPSVA GFSKTGERLV GQVAKRQMIS
NSERTIASIK RRMGSNYKVN IDDKEYTPQE ISAMILQKLK TDAESYLGEK IEKAIITTPA
YFTDAQRQAT KDAGRIAGLE VLRIINEPTA AALAYGLDKD KDHTVLVFDL GGGTFDVSIL
ELGEGIFEVK ATSGNNLLGG DDFDQRIVDW LVAEFKKDTG IDLHHDRMAM QRLREAAEKA
KIELSGVTTT NINLPFITAD ANGPKHLDTN LTRAKFEDLT ADLVERTMGP TRQALADAGL
EPKDIDKILL VGGSTRTPAV QEAIRNILGK EPHKGINPDE CVAVGAAIQA GVLAGEVKDV
LLLDVTPLSL GIETLGNVFT RLIERNTTIP TSKSQIFSTA ADGQTTVEIH VLQGERPMAS
DNKTLGKFLL TGIPPAPRGV PQIEVKFDID VNGIVNVSAK DLGTGRAQSI TITGTSSLSE
EEIKRMVREA EQKAEEDRRR KEEADLRNQA DSMIYQAEKT IKDLGDKAEQ SKVEQVNRAV
AELREALQGT DLELIRQKMD NLTTPLYEMS AAMYQQQTEK AQQNQQGFDQ GQTAGSEEKK
EEVVDADYEI KDEK
//
