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PKN2_MYXXA
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   03-AUG-2022, entry version 114.
DE   RecName: Full=Serine/threonine-protein kinase pkn2;
DE            EC=2.7.11.1;
GN   Name=pkn2;
OS   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; 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   RefSeq; WP_011556352.1; NZ_FNOH01000001.1.
DR   AlphaFoldDB; P54736; -.
DR   SMR; P54736; -.
DR   GeneID; 41363630; -.
DR   OMA; VMLTDIQ; -.
DR   BRENDA; 2.7.11.1; 3551.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; -; 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   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   SUPFAM; SSF56112; SSF56112; 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
 
 
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