ID A0A134CA72_9FIRM Unreviewed; 621 AA.
AC A0A134CA72;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=HMPREF3191_01530 {ECO:0000313|EMBL:KXB89085.1};
OS Veillonellaceae bacterium DNF00626.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae.
OX NCBI_TaxID=1588754 {ECO:0000313|EMBL:KXB89085.1, ECO:0000313|Proteomes:UP000070542};
RN [1] {ECO:0000313|EMBL:KXB89085.1, ECO:0000313|Proteomes:UP000070542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00626 {ECO:0000313|EMBL:KXB89085.1,
RC ECO:0000313|Proteomes:UP000070542};
RA Oliw E.H.;
RL Submitted (JAN-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}.
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:KXB89085.1}.
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DR EMBL; LSDR01000103; KXB89085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A134CA72; -.
DR STRING; 1588754.HMPREF3191_01530; -.
DR PATRIC; fig|1588754.3.peg.1490; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000070542; 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:UP000070542};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 473..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 621 AA; 67039 MW; D962F9A36DB74B45 CRC64;
MSKVIGIDLG TTNSVVAVME GGEPVVISNT EGSRLTPSVV GFSKTGERLI GQLAKRQAVS
NPARTIVSIK RHMGETGYKV KIDDKEYTPQ EISAMILQKL KADAEAYLGE SVTDAVITCP
AYFTDSQRQA TKDAGAIAGL NVLRIINEPT ASALAYGLDK LKDGKEHRFL VYDLGGGTFD
VSILNLADGV FEVEASHGNG HLGGDDFDAR VMDWIGTTFK AQNGFELKRD PMTNQRLKEA
AEKAKIELSN VMSTDINLPF ITMDANGQPV HFDATLTRAM FDKITEDLVK ETVEPIDIAL
KDAGLTVNDI DKVLLVGGSS RIPAVQTLVK EKFGKEPSKS VNPDESVAVG AAVQAGVLKG
DVKDVLLLDV TPLSLGIETL GGVFTTMIKR NTTIPASKSQ VFSTASDNQP SVDIHVLQGE
RPMAANNKTL GRFELADIPP APRGVPQIQV TFDIDANGIV HVSAKDLGTG KEQKIDIKSS
SGLSDEEIER MQQDAKAHEE EDKKRKDLIE ERNKGEALIY QAQKTIKDLG DKADAAKVKE
INDAIAVLQE TLKGEDVEKM KSDSEALTKP LYDLTSQMYQ QAQQAQQAAG AENAGANKEA
QDKAKDNVVD ADYKVVDDDK K
//
