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Database: UniProt
Entry: D1AVP3_STRM9
LinkDB: D1AVP3_STRM9
Original site: D1AVP3_STRM9 
ID   D1AVP3_STRM9            Unreviewed;       602 AA.
AC   D1AVP3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 81.
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   OrderedLocusNames=Smon_1358 {ECO:0000313|EMBL:ACZ01803.1};
OS   Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS   9901).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Streptobacillus.
OX   NCBI_TaxID=519441 {ECO:0000313|EMBL:ACZ01803.1, ECO:0000313|Proteomes:UP000002072};
RN   [1] {ECO:0000313|EMBL:ACZ01803.1, ECO:0000313|Proteomes:UP000002072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901
RC   {ECO:0000313|Proteomes:UP000002072};
RX   PubMed=21304670; DOI=10.4056/sigs.48727;
RA   Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA   Del Rio T.G., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA   Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C.,
RA   Ovchinikova G., Pati A., Mavromatis K., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Chain P.;
RT   "Complete genome sequence of Streptobacillus moniliformis type strain
RT   (9901T).";
RL   Stand. Genomic Sci. 1:300-307(2009).
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; CP001779; ACZ01803.1; -; Genomic_DNA.
DR   RefSeq; WP_012859349.1; NC_013515.1.
DR   AlphaFoldDB; D1AVP3; -.
DR   STRING; 519441.Smon_1358; -.
DR   GeneID; 29674046; -.
DR   KEGG; smf:Smon_1358; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_0; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000002072; 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; 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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000002072};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          578..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          486..553
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   602 AA;  65329 MW;  2759CE382048DE0B CRC64;
     MSKIIGIDLG TTNSCVSVME GGTFTIIPNS EGERTTPSVV SIESNGEIIV GSTAKRKAIT
     EPKQTVISIK THMGSDHKVD IHGKSYTPQE ISAMILKKLK KDAESYLGET VKEAVITVPA
     YFTDAQRQAT KDAGEIAGLE VKRIINEPTA AALAYGMDKE KEEKILVFDL GGGTFDVSVL
     EVGAGLVEVK ATAGNNHLGG DDFDAAIINW LADEFKKETG IDLRNEPQAY QRLKDAAEDA
     KKKLSSTLET TISLPFIAMD ATGPKNLEKK LTRAAFNELT KHLVEKTKEP VKQALLDAGY
     TVRDIEQVLL VGGSTRIPAV QEWVKEYFGK EPNRSINPDE VVSVGAAIQG GVLGGNVKDV
     LLLDVTPLSL GIETMGGVFT KMIERNTTIP TKKSQVYSTA ADNQTAVTIH VLQGERAQAS
     QNHTLGQFNL EGIPAAPRGI PQIEVTFDID SNGIVHVTAK DLGTGKENQV TISGSSNLSK
     DDVERMKKEA EANEEADNKF RELIEARNMA DHLIISTEKT IKENEDKLEG NEKENIEKAI
     EELKKVKDSE NIEEIRKGIE GLSKASEAFA MRIYQAAQAA QQPASENAEN NNDDVVEAEE
     VK
//
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