ID   PKN5_MYXXA              Reviewed;         380 AA.
AC   P54737;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Serine/threonine-protein kinase pkn5;
DE            EC=2.7.11.1;
GN   Name=pkn5;
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=8733241; DOI=10.1111/j.1365-2958.1996.tb02630.x;
RA   Zhang W., Inouye M., Inouye S.;
RT   "Reciprocal regulation of the differentiation of Myxococcus xanthus by Pkn5
RT   and Pkn6, eukaryotic-like Ser/Thr protein kinases.";
RL   Mol. Microbiol. 20:435-447(1996).
CC   -!- FUNCTION: Pkn5 and pkn6 may have reciprocal roles in growth and
CC       development. Pkn5 may be a kinase that negatively regulates
CC       development.
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: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed constitutively throughout the life
CC       cycle, with slight increases at an early stage of development.
CC   -!- PTM: Autophosphorylated on serine residues.
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; U40656; AAB40049.1; -; Genomic_DNA.
DR   PIR; S70964; S70964.
DR   RefSeq; WP_011552619.1; NZ_JABFNQ010000027.1.
DR   AlphaFoldDB; P54737; -.
DR   SMR; P54737; -.
DR   PRIDE; P54737; -.
DR   GeneID; 41359927; -.
DR   OMA; PSMAPMW; -.
DR   BRENDA; 2.7.11.1; 3551.
DR   GO; GO:0005737; C:cytoplasm; 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; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..380
FT                   /note="Serine/threonine-protein kinase pkn5"
FT                   /id="PRO_0000171230"
FT   DOMAIN          9..378
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          100..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        244
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   380 AA;  41924 MW;  DC3ADFB24420C1F1 CRC64;
     MPLKVIGPYR VLETLGSGGA GTVYRALDRR TTDEVALKLL SAGPARDARA ARRLAREFDT
     LVDLSHPNVV KVFESGVHQG VPYLAMELIE GLTLRHYLDL SSGDRQTPPG SHTPRSPLSV
     LRTADDDFGP LSRSFSDSMD DSEDSPFDGT FGLEAFAEEA PSEDLESFAS SASPHVGIGS
     DDSLEGFDLP PPMPRPAEPE EEPGRVVREE DLNRPERMGR LKDAMLQICE ALAYIHGHGL
     VHRDLKPSNI MVDDDRQVRL MDFGLAKFLA DDAAITEAGK LVGTYRYMAP EQILGEPLDG
     RADLYSLGVI LYELLSGRPP FDAKTPHELW RQVLETEPPP VLALNLHGDP QLARVAHRLI
     RKEPDDRFQT AEEVYEALSE