PKN6_MYXXA
ID PKN6_MYXXA Reviewed; 710 AA.
AC P54738;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Serine/threonine-protein kinase pkn6;
DE EC=2.7.11.1;
GN Name=pkn6;
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. Pkn6 may be a transmembrane sensor of external signals for
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: Cell membrane; Single-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expressed constitutively throughout the life
CC cycle, with slight increases at an early stage of development.
CC -!- PTM: Autophosphorylated on serine and threonine 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; AAB40050.1; -; Genomic_DNA.
DR PIR; S70965; S70965.
DR RefSeq; WP_011552620.1; NZ_JABFNQ010000027.1.
DR AlphaFoldDB; P54738; -.
DR SMR; P54738; -.
DR PRIDE; P54738; -.
DR GeneID; 41359928; -.
DR OMA; PVGAYQI; -.
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: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; IPR013229; PEGA.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF08308; PEGA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..710
FT /note="Serine/threonine-protein kinase pkn6"
FT /id="PRO_0000171231"
FT TOPO_DOM 1..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..710
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 6..280
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 337..348
FT /note="1"
FT REPEAT 358..369
FT /note="2"
FT REGION 308..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..369
FT /note="2 X 12 AA repeats of P-[VA]-D-S-T-S-P-T-T-P-M-P"
FT REGION 404..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 12..20
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 710 AA; 74622 MW; EDCF670072DCBEAA CRC64;
MQIGKYQLVR KLASGGMAEV FLAKAAGPRG FEKTLVLKRI LPHLAEDAAF VEMFLGEARL
AAQLEHPNIV QIFDFGEAEG SFFLAMEFID GPNLRKLVKR AAEEALPPAF CAKVVAAAAE
GLAYAHEFRD VETGEPLGLI HRDVSPDNIL VSRQGAVKVV DFGIAKVAGQ GHRTLTGVVK
GKVAYMPPEQ LQAKAMDRRV DVYALGVVLY ELLTGKRPFD ATTDVSVMQA ILFESFIPVS
ARRPDVPVAL QQVLDKALAK DRERRYADCR ALQDDLERFV LSTGEPVGAY QIAQRIAQWV
PEVAAAPAMT PSQGGSKGAV ASQAKADARS ASMVSPPVDS TSPTTPMPRS LVAPVEVPAD
STSPTTPMPV AIGGVVQALE PRSSPQQDTL QSYPVVVKTP ALRADASARG ASRPRAQSRA
SGVKVQAPQA RDEDVVAMAA ASSPPSGGAS PAPTTPEDAD DAVHTRSTEY AATVPSGRPG
GRIAGIVGAV VALLVGGAVT VMRGDDSEVS PVRVNPPPLT HLPREPAVPS QGGRNVPQEK
PAANVNAGAR DSNDGAQAKP QVSTDVSVVP QEPHVARDAT TPEAGLPTVK DAPPENGGAA
SKEGSAVVAK REPAKASGDP EPNPSRVRER APTQKVAAVA KGRLEFRIRP YAVVSLDGKV
LGQTPFAAVE VPEGRHTVRL VNKELGKDVT RTVDVKAGQA TVFKLNLEAE
