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Database: UniProt
Entry: B5GB62_STRSH
LinkDB: B5GB62_STRSH
Original site: B5GB62_STRSH 
ID   B5GB62_STRSH            Unreviewed;       807 AA.
AC   B5GB62;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=SSBG_01520 {ECO:0000313|EMBL:EDY43558.3};
OS   Streptomyces sp. (strain SPB074).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY43558.3, ECO:0000313|Proteomes:UP000002779};
RN   [1] {ECO:0000313|Proteomes:UP000002779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA   Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA   Galagan J., Nusbaum C., Birren B.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDY43558.3, ECO:0000313|Proteomes:UP000002779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces sp. strain SPB74.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; GG770539; EDY43558.3; -; Genomic_DNA.
DR   AlphaFoldDB; B5GB62; -.
DR   Proteomes; UP000002779; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.40.10.480; -; 1.
DR   Gene3D; 2.40.128.630; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR22983; PROTEIN KINASE RELATED; 1.
DR   PANTHER; PTHR22983:SF6; SERINE_THREONINE-PROTEIN KINASE 36; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   Pfam; PF13570; PQQ_3; 3.
DR   SMART; SM00564; PQQ; 9.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EDY43558.3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          40..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          321..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..350
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   807 AA;  84642 MW;  50283D0A4A4548F6 CRC64;
     MAVHRGGRCA GAALVVPDGE AAEEEMDQLT QHDPRRIGQF EVLGRLGAGG MGLVYMARSA
     SGRRVAIKTV RAELAQDQLF RVRFTREVEA ARAVSGFYTA AVVDADPRAA VPWLATAYVP
     APSLEEIVNE CGPLPANAVR WLAAGVAEAL ESIHGAGLVH RDLKPSNVLV MHDGPRVIDF
     GIASGVSNTR LTMTNVAVGT PAYMSPEQAK DSRSVTGASD VFSLGSTLVF AATGHAPFHG
     ANPVETVFML LREGPDTEGM PEELQPLIES CMGMEAAMRP SPADLQASLS PHLFAAGADD
     SGTASAWLPP RAVALIESKS RTGIGPRQPA PPRPVPPSPP VPPRPAVEPV VPEQPGKHAA
     EPEVLLPGTR VPVREGPRLA EARATGEAER QAGHLALASR WTRESNRRAP VAAPPTTAAT
     EPRPGGPGQP WRPWRFRMSN DVWGTPVLAD DLVYVTSFEV HALDVATGRR RFKTRDVALV
     MAVDQGRIHA SDGPGVHALD SRTGAEIWRA AAPGWVYALA AGRGTVLTAS RGGTVRGWDA
     ASGERLWEAG GLQTDFETAE AAPVLHEGTA YLWQDARLRA VDARTGTERW SYPVGDVSAC
     GGVPPRVTAA ADGSVYVCAG TRVLAIEAHS GRVRWQFEAP AVFLSPPAFA PGPAVTGGGV
     YVADYHGAVW ALDAEDGRDR WRIATEARSS VDPVLVAGGL VHVASGNGMY TLNAVHGTPA
     WRFQAGGDIV GAPVASGDLL HFGSADNCLY TLSASGGQLR WKLLTGGAVT GSPVVRGGVV
     YACSGDRCVY ALDAKEGTGT QSAQGRG
//
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