ID Q8DVK1_STRMU Unreviewed; 616 AA. AC Q8DVK1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=pknB {ECO:0000313|EMBL:AAN58230.1}; GN OrderedLocusNames=SMU_484 {ECO:0000313|EMBL:AAN58230.1}; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58230.1, ECO:0000313|Proteomes:UP000002512}; RN [1] {ECO:0000313|EMBL:AAN58230.1, ECO:0000313|Proteomes:UP000002512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512}; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H., RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.; RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental RT pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002). 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}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004167}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014133; AAN58230.1; -; Genomic_DNA. DR RefSeq; NP_720924.1; NC_004350.2. DR RefSeq; WP_002263039.1; NC_004350.2. DR AlphaFoldDB; Q8DVK1; -. DR SMR; Q8DVK1; -. DR STRING; 210007.SMU_484; -. DR KEGG; smu:SMU_484; -. DR PATRIC; fig|210007.7.peg.424; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2815; Bacteria. DR HOGENOM; CLU_000288_135_2_9; -. DR OrthoDB; 9788659at2; -. DR PhylomeDB; Q8DVK1; -. DR Proteomes; UP000002512; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR CDD; cd06577; PASTA_pknB; 2. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.30.10.20; -; 3. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR005543; PASTA_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR NCBIfam; NF033483; PknB_PASTA_kin; 1. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1. DR Pfam; PF03793; PASTA; 3. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00740; PASTA; 3. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51178; PASTA; 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}; Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW Cell division {ECO:0000256|ARBA:ARBA00022618}; KW Kinase {ECO:0000313|EMBL:AAN58230.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002512}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AAN58230.1}; KW Transferase {ECO:0000313|EMBL:AAN58230.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 344..364 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 12..273 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 366..433 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT DOMAIN 502..579 FT /note="PASTA" FT /evidence="ECO:0000259|PROSITE:PS51178" FT REGION 309..336 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 578..616 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 42 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 616 AA; 66914 MW; 47DBCBEF853457A6 CRC64; MIQIGKLFAG RYRILQSIGR GGMADVYLAN DLILDNEEVA IKVLRTNYQT DQVAVTRFQR EARAMAELNH PNIVAIRDIG EEDGQQFLAM EYVDGADLKK YIQDHAPLSN AEVIRIMKEV LSAMTLAHQK GIIHRDLKPQ NVLLTKDGTA KVTDFGIAVA FAETSLTQTN SMLGSVHYLS PEQARGSKAT VQSDIYAMGI MLFEMLTGHI PYDGDSAVTI ALQHFQKPLP SIIAENKNVP QALENVVIKA TAKRLTDRYH STQEMLQDLR TSLQPNRSRE RKLVFSDASD TKPLPKLEQA AANSLAAQSL KNKTSNQDKV DHKSKPKTKP QPKPKKKRHF LARFFKIFFI LVAIGIAVLT YLVLTKPSTV SVPDVSGDKL STAKMIIRKS GLKVGDVQKI EDDNVGAGKV VRTNPSAGSK KREGSSVDIF VASAKGFKME DYTGQDYKDA IDNLTNNYGV SRDSIVLKEV SSDDYSGGTV IGQSPKPGKT YHPSSDKKIT LKVVKVTMPN LKNSTYEEAV STLTAMGISS SRIKAYDASD YSSEISSPSS SSLVVGQSPY YGNTVSLSSN DDIILYVSTS GGSHSGSSSS ESSNSEGTTS SEASTDSSSS ATTTSH //