ID PKNS_MYCGE Reviewed; 387 AA. AC P47355; Q49450; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 129. DE RecName: Full=Putative serine/threonine-protein kinase; DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159}; GN OrderedLocusNames=MG109; OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) OS (Mycoplasmoides genitalium). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-262 AND 286-376. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random sequencing."; RL J. Bacteriol. 175:7918-7930(1993). RN [3] RP SEQUENCE REVISION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=16407165; DOI=10.1073/pnas.0510013103; RA Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R., RA Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.; RT "Essential genes of a minimal bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006). 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 -!- 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; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane CC protein {ECO:0000255}. CC -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a CC global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; L43967; AAC71327.2; -; Genomic_DNA. DR EMBL; U01720; AAC43195.1; -; Unassigned_DNA. DR EMBL; U01748; AAD10561.1; -; Genomic_DNA. DR RefSeq; WP_009885667.1; NZ_AAGX01000002.1. DR AlphaFoldDB; P47355; -. DR SMR; P47355; -. DR STRING; 243273.MG_109; -. DR KEGG; mge:MG_109; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_700090_0_0_14; -. DR InParanoid; P47355; -. DR OrthoDB; 9788659at2; -. DR BioCyc; MGEN243273:G1GJ2-122-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1. DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..387 FT /note="Putative serine/threonine-protein kinase" FT /id="PRO_0000171201" FT TRANSMEM 232..252 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 363..383 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 15..344 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 164 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 21..29 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 387 AA; 44626 MW; 346D35DDF2C15610 CRC64; MEAILKIGDI VENKYQIEKL LNRGGMDSYL FLAKNLNLKN YGPVQKKQYG HLVLKVVQKN PKINENNWKK FLDEMVTTTR VHHSNLVKSF DVVNPFLKIV RGNKTIALNQ IVMIAMEYVD GPSLRQLLNR KGYFSVSEVV YYFTKIVKAI DYLHSFKHQI IHRDLKPENI LFTSDLTDIK LLDFGIASTV VKVAEKTEVL TDENSLFGTV SYMIPDVLES TVNKAGKKVR KPPNAQYDIY SLGIILFEML VGRVPFNKSI NPNKERETIQ KARNFDLPLM QATRSDIPNS LENIAFRCTA VKRENNKWLY SSTKELLEDL ANWENEQAMI KPANERVLEG QVEIREMMLE KPLAWYFKTW ALSIFTIVFI GLIIAAIVLL LIFNARF //