ID A0A068NK78_9ACTO Unreviewed; 625 AA.
AC A0A068NK78;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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:AIE83150.1};
GN ORFNames=FB03_07715 {ECO:0000313|EMBL:AIE83150.1};
OS Actinotignum schaalii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE83150.1, ECO:0000313|Proteomes:UP000035032};
RN [1] {ECO:0000313|EMBL:AIE83150.1, ECO:0000313|Proteomes:UP000035032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE83150.1,
RC ECO:0000313|Proteomes:UP000035032};
RX PubMed=25189588;
RA Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M.,
RA Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M.,
RA Christensen J.J., Prag J., Thomsen T.R.;
RT "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420.";
RL Genome Announc. 2:e00880-14(2014).
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}.
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DR EMBL; CP008802; AIE83150.1; -; Genomic_DNA.
DR RefSeq; WP_026428617.1; NZ_JASOPO010000004.1.
DR AlphaFoldDB; A0A068NK78; -.
DR GeneID; 81702282; -.
DR KEGG; asg:FB03_07715; -.
DR Proteomes; UP000035032; Chromosome.
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; 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 497..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 229..256
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 497..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 625 AA; 66663 MW; 78E19A0D587DA10F CRC64;
MARAVGIDLG TTNSVVAVLE GGEPTVIANA EGARTTPSVV GFSKSGEVLV GEVAKRQAVT
NVDRTISSVK RHMGDDWKVD IDGKDYNAQQ ISAFILQKLK KDAEAYLGDT VTDAVITVPA
YFNDAQRQAT KDAGTIAGLN VQRIVNEPTA AALAYGLEKG KEDETILVFD LGGGTFDVSL
LEVGKDEDDF SFIQVKATSG DNKLGGDDWD QRIVNWLVDQ VKNASGVDLS KDKIALQRLK
EAAEKAKIEL SAATSTQISL PYISMSESGP IHVDETLSRA KFEDMTKDLL DRTKTPFMNV
IRDAGIQISD IDHVVLVGGS TRMPAVTEVV KELTNGREPN KGVNPDEVVA VGAALQSGVI
TGDRKDVLLI DVTPLSLGIE TKGGVMTKLI QRNTAIPTKH SETFSTAEDN QPSVSIQVFQ
GEREFTRDNK PLGTFDLTGI APAPSGVPQI EVTFDIDANG IVHVSARDKS TGKEQSMTIT
GGSALSEEEI NRMVKEAEEH AAEDAKAKEE TDTRNQAEQT AYSIERLIKD NKDKLTDATV
TEVEEAIAKV RETLKGTGNV EDVKSALAEL NEKSQKIGQE IYAQAQAAEQ NGGANASGAA
GGSGASGSSD DNIVDAEVVD DEENK
//