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Database: UniProt
Entry: Q1DDI7_MYXXD
LinkDB: Q1DDI7_MYXXD
Original site: Q1DDI7_MYXXD 
ID   Q1DDI7_MYXXD            Unreviewed;       710 AA.
AC   Q1DDI7;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Capsular exopolysaccharide family protein {ECO:0000313|EMBL:ABF90823.1};
GN   OrderedLocusNames=MXAN_1025 {ECO:0000313|EMBL:ABF90823.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF90823.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF90823.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   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).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001074};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the etk/wzc family.
CC       {ECO:0000256|ARBA:ARBA00008883}.
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DR   EMBL; CP000113; ABF90823.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1DDI7; -.
DR   STRING; 246197.MXAN_1025; -.
DR   EnsemblBacteria; ABF90823; ABF90823; MXAN_1025.
DR   KEGG; mxa:MXAN_1025; -.
DR   eggNOG; COG0489; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   HOGENOM; CLU_009912_2_1_7; -.
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:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05387; BY-kinase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR032807; GNVR.
DR   InterPro; IPR003856; LPS_length_determ_N_term.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005702; Wzc-like_C.
DR   NCBIfam; TIGR01007; eps_fam; 1.
DR   PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR   Pfam; PF13614; AAA_31; 1.
DR   Pfam; PF13807; GNVR; 1.
DR   Pfam; PF02706; Wzz; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          3..94
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          366..437
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          520..669
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   710 AA;  78360 MW;  D63F46ADF837EBFC CRC64;
     MQYVRAVWRR KWVVLGVAVV VAALTAAHTL RQPKVYSASA SLIIDVMAPR FLDGEVKEVM
     GEERSNYWFN KEYYATQSQI ITSRAVAGRV VDKLGLSTDA DFLGMAHITD EKTRLQAMQG
     ADAVALVQSR IRVIPARDSR VMNIAVDDFD ARRAALLANE VAAAYMAENL ALKLRTTEDA
     RDWLEIRLAE LESQSKTSEL AVYDFKKDAD MLSTSLESRM SIVSERINSF NLKLTEVRIQ
     IAAQQARVEA IHRLRKASPE DETWAEALSG ASDGPIQDLR RSYTELRMTC AELGERYLSE
     HPKLLECNRK LSVVREDFLK SLSNVVRSAE TSLAESVAQE KNLVRLLDAE KSEAFLVNKK
     AIEFDRLKRD SDNNQRLYEL VARRLKDIEL SGMLRTSNVR VLDPARPILV PVKPHVRRNL
     AVGLVMGLLA GLGVVLLLEL LENSVATQAD VEERLGLAFL GVMPRLDGSK APRERDLHVH
     REPKSTAAEC CRAIRTNLLF MSPDNPFKTL VVTSSGPQEG KSTTCINLGV AMAQSGNRVL
     LLDTDMRRPR LHRAFGVPNE LGISSLVVGE GTLDAAVKST EVPGLFVLPC GPLPPNPAEL
     LHTQAFTDLL KAASERFDRV ILDSPPINAV ADAAVLATKC DGVVLVLKAA KTNRESARRA
     LRSLADVQAR MYGAILNDVD LSAPRYGDSY LGYQGYGQYA EDSKDGVAQS
//
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