ID PKN2_MYXXA Reviewed; 830 AA.
AC P54736;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Serine/threonine-protein kinase pkn2;
DE EC=2.7.11.1;
GN Name=pkn2;
OS Myxococcus xanthus.
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DZF1;
RX PubMed=7774814; DOI=10.1101/gad.9.8.972;
RA Udo H., Munoz-Dorado J., Inouye M., Inouye S.;
RT "Myxococcus xanthus, a Gram-negative bacterium, contains a transmembrane
RT protein serine/threonine kinase that blocks the secretion of beta-lactamase
RT by phosphorylation.";
RL Genes Dev. 9:972-983(1995).
CC -!- FUNCTION: Regulates the activity of endogenous beta-lactamase or
CC related enzymes, by blocking their secretion by phosphorylation, in
CC response to an external signal yet to be identified.
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:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M94857; AAA98813.1; -; Genomic_DNA.
DR PIR; A57060; A57060.
DR AlphaFoldDB; P54736; -.
DR SMR; P54736; -.
DR OMA; VMLTDIQ; -.
DR BRENDA; 2.7.11.1; 3551.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
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; IEA:UniProtKB-KW.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07302; CHD; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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 Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..830
FT /note="Serine/threonine-protein kinase pkn2"
FT /id="PRO_0000171228"
FT TOPO_DOM 1..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..830
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 13..283
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 396..511
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 296..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 830 AA; 87680 MW; BD53F33CE057FA1F CRC64;
MLAPDSLVLD GRFRVLRPLG SGGMGEVYLG EQVSLGRKVA IKVLHHDLHA QAGMAERFKR
EARLLSAVEH PAVVRIVDFG ESGDHACLVM EFVEGESLYD VLTPGPMPPG RALPLLQQLA
EGLAAIHDKG IIHRDLKPEN VFISKSARGE QARLLDFGIA RLVEPDAASS VSQIGVVLGT
PEYLSPEQAV GAKVDTRSDL YSFGVLTYRV LSGRLPFDGP LPRNFLSQHA SAAPLPLDRA
APTLSRYVGL LSLVMRLLEK DASKRPQSAH ELADALAAAH SALSAFTPGL GTPAYVPQPG
SGATPSSGTS VFGTGSASGS SSGPTGTAAF AGVAPAPQAS SGTAAFGVAS SSGSASGALP
AASPHTGTAS FGLKSSGGVA AVTGGNASVV KPQNLTVMLT DIQGFTERTS RQTHEENARM
LETHDKLLMP LVKEHDGRLV QKRGDALLVV FRSPTAGVLC GMAMQDRLWR HNQTVPEVDR
LNVRVCLHAG EVLATPDSVL GEPMEVIEAV EHVASAGEVT FTEAVNLARN RAEATAEPCG
AITLPGRNEQ LQLYRCQRAA EGPPFGDRFA SQGSRGNALA PLLAKLQAVK LPTGLGELLR
QRRREAALVA GAVVLLGAGA AWLSQRNDAG TRAFALLEDG KLNEALALMD AATDEEKELP
SLRRARVAAN HAKGHHISER TALSHLKEEE LEDVEPLILD GLAEDYGKEP LTVLGNALAR
FPKDRLRAHY EDLAEEAYSL RQWGALRYLE FVKAADGVNL VRAYSEALNS PDCDIRTQAA
NRLAGLGDAD AIPAMERVTS LPKAKGLLGS KDCGHEAAAT AIKSLKQKSD
//
