ID   MASK_MYXXD              Reviewed;         646 AA.
AC   Q1DB00; Q93S46;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Tyrosine-protein kinase MasK;
DE            EC=2.7.10.2;
GN   Name=masK; OrderedLocusNames=MXAN_1929;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2464581; DOI=10.1128/jb.171.2.819-830.1989;
RA   Stephens K., Hartzell P.L., Kaiser D.;
RT   "Gliding motility in Myxococcus xanthus: mgl locus, RNA, and predicted
RT   protein products.";
RL   J. Bacteriol. 171:819-830(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN   [3]
RP   CHARACTERIZATION, AND INTERACTION WITH MGLA.
RX   PubMed=12453225; DOI=10.1046/j.1365-2958.2002.03258.x;
RA   Thomasson B., Link J., Stassinopoulos A.G., Burke N., Plamann L.,
RA   Hartzell P.L.;
RT   "MglA, a small GTPase, interacts with a tyrosine kinase to control type IV
RT   pili-mediated motility and development of Myxococcus xanthus.";
RL   Mol. Microbiol. 46:1399-1413(2002).
CC   -!- FUNCTION: Essential for growth. Interacts with MglA to control social
CC       gliding motility.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Interacts with MglA. {ECO:0000269|PubMed:12453225}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF377950; AAK54653.1; -; Genomic_DNA.
DR   EMBL; CP000113; ABF90801.1; -; Genomic_DNA.
DR   RefSeq; WP_011552028.1; NC_008095.1.
DR   AlphaFoldDB; Q1DB00; -.
DR   SMR; Q1DB00; -.
DR   STRING; 246197.MXAN_1929; -.
DR   EnsemblBacteria; ABF90801; ABF90801; MXAN_1929.
DR   GeneID; 41359343; -.
DR   KEGG; mxa:MXAN_1929; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_151_5_7; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR049806; MasK-like_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   NCBIfam; NF033768; myxo_SS_tail; 1.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   CHAIN           1..646
FT                   /note="Tyrosine-protein kinase MasK"
FT                   /id="PRO_0000282835"
FT   TOPO_DOM        1..415
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        434..646
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..300
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          373..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         31..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   646 AA;  68576 MW;  C9667634284FE40C CRC64;
     MSPPQTTLPV TEAGLVPLLQ PYGPYVLVRK LAEGGMAEIF LAKLLGADGF ERNVVIKRML
     PHLTNNPDFV EMFRDEARLA AKLAHPNIVQ IQELGFAEGC YYICMEYLAG EDFSTTLRLA
     GRKRHYVPLP VVLRVLIDAA RGLHFAHEFT NEAGQPLNVV HRDISPSNLY LTYQGQVKVL
     DFGIAKAESR LVNTRTGVVK GKYMYMAPEQ ARGKEVDRRA DIFALGVSLY EALTHVRPFS
     RENDLAVLNA LLQGELKPPR ELRPDLPEEL EAILLKAMAF KPEDRYPTAE AFADALETFL
     SEHLSGSGAM PLGAFLKGHF GEERFTERSR IPTLATLTAT YGGAAAGAQG QAPGAEPHGT
     NLYGVLAREG DATSAQRPGM SMRPSSPGVP AHGAASRGST SPESAPTAGG RRWRTLAVGL
     AGGLMLAAAG IVGYRQWMTT PASVSLVPAT VPVVEAVAPE AAAAQVGAPM EAVAPVGAAA
     QAGSLTDAVA NGAGGDVGET DSAQLSVDAA GVTETDEAGL AGAASDVEAE ADEEGADAAP
     VRSKKASSQK RVTLGIDDVQ RVVSRGRARI TTCFERYKAD LPSSQGEVQV QLTIVSSGKV
     RAGTRGPLAS SGVGRCLEAQ AERLRFPPHR DQEVTVVMPF SWRVTQ
//