MASK_MYXXD
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 03-AUG-2022, entry version 102.
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; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; 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 OMA; YICMEYL; -.
DR OrthoDB; 1377603at2; -.
DR Proteomes; UP000002402; Chromosome.
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:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 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
