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Database: UniProt
Entry: A0A068NK78_9ACTO
LinkDB: A0A068NK78_9ACTO
Original site: A0A068NK78_9ACTO 
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
//
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