ID A0A1H8YZ29_9FIRM Unreviewed; 627 AA.
AC A0A1H8YZ29;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN02910382_00294 {ECO:0000313|EMBL:SEP57331.1};
OS Butyrivibrio sp. TB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520809 {ECO:0000313|EMBL:SEP57331.1, ECO:0000313|Proteomes:UP000198682};
RN [1] {ECO:0000313|EMBL:SEP57331.1, ECO:0000313|Proteomes:UP000198682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TB {ECO:0000313|EMBL:SEP57331.1,
RC ECO:0000313|Proteomes:UP000198682};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOER01000002; SEP57331.1; -; Genomic_DNA.
DR RefSeq; WP_022755276.1; NZ_FOER01000002.1.
DR AlphaFoldDB; A0A1H8YZ29; -.
DR Proteomes; UP000198682; 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; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
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; 2.
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 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 584..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 535..575
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 627 AA; 67456 MW; AB90FD90B40DB173 CRC64;
MGKIIGIDLG TTNSCVAVME GGKPTVIANA EGARTTPSVV AFTKNGERLV GEPAKRQAVT
NADHTISSIK RDMGTDNGRN IDGKKYSPEQ ISAMILQKLK KDAEDYLGES VSQAVITVPA
YFNDAQRQAT KNAGKIAGLE VERIINEPTA AALAYGLDNE KEQKIMVYDL GGGTFDVSII
EIGDGVIEVL STNGDTHLGG DDFDNRIIDW MVEEFKAKEG VDLSGDKMAM QRLKEAAEKA
KKELSSSTTT NINLPFITAT AEGPKHFDMD LTRAKFEELI HDLVERTAIP VQNAMRDAGL
TNADLGKVLL VGGSTRVPCV VEKVKQLTGQ EPSKNLNPDE CVAVGAGIQG GKLNNEAGTG
DILLLDVTPL SLSIETMGGI ATKLIERNTT IPTKKSQIFS TAADNQTAVD INVLQGERQF
ARDNKSLGQF RLDGIPPARR GMPQIEVTFD IDANGIVNVS AKDLGTGKEQ HITITSGTNM
SDDDIDKAIK EAQEYEAQDK KRKEGIDARN EADSFVFQTE QALKDAGDKI DATAKSTVEA
DLTDLKATLD ATKDKELTDE EIDKIKTQKE KLMTDAQQLF SKMYENMQQQ AGPQAGPQAG
PGPDMGGAAG SQTQNNDDVV DGDYREV
//
