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WZC_SALTY
ID   WZC_SALTY               Reviewed;         719 AA.
AC   Q9F7B1;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Tyrosine-protein kinase wzc;
DE            EC=2.7.10.-;
GN   Name=wzc; OrderedLocusNames=STM2116;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=11004393; DOI=10.1111/j.1574-6968.2000.tb09312.x;
RA   Stevenson G., Lan R., Reeves P.R.;
RT   "The colanic acid gene cluster of Salmonella enterica has a complex
RT   history.";
RL   FEMS Microbiol. Lett. 191:11-16(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Required for the extracellular polysaccharide colanic acid
CC       synthesis. The autophosphorylated form is inactive. Probably involved
CC       in the export of colanic acid from the cell to medium (By similarity).
CC       {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Dephosphorylated and activated by wzb.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. Seems to be phosphorylated through a
CC       cooperative two-step mechanism. First, Tyr-568 is phosphorylated in an
CC       intramolecular reaction that generates a significant increase of
CC       protein kinase activity. Then Tyr-707, Tyr-709, Tyr-710, Tyr-712 and
CC       Tyr-714 are phosphorylated in an intermolecular Tyr-568-dependent
CC       reaction (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the etk/wzc family. {ECO:0000305}.
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DR   EMBL; AF285084; AAG24806.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21020.1; -; Genomic_DNA.
DR   RefSeq; NP_461061.1; NC_003197.2.
DR   RefSeq; WP_000136405.1; NC_003197.2.
DR   AlphaFoldDB; Q9F7B1; -.
DR   SMR; Q9F7B1; -.
DR   STRING; 99287.STM2116; -.
DR   PaxDb; Q9F7B1; -.
DR   EnsemblBacteria; AAL21020; AAL21020; STM2116.
DR   GeneID; 1253637; -.
DR   KEGG; stm:STM2116; -.
DR   PATRIC; fig|99287.12.peg.2238; -.
DR   HOGENOM; CLU_009912_0_0_6; -.
DR   OMA; QQIYIQL; -.
DR   PhylomeDB; Q9F7B1; -.
DR   BioCyc; SENT99287:STM2116-MON; -.
DR   BRENDA; 2.7.10.1; 5542.
DR   UniPathway; UPA00631; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR005702; EPS_synthesis.
DR   InterPro; IPR032807; GNVR.
DR   InterPro; IPR003856; LPS_length_determ_N_term.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13614; AAA_31; 1.
DR   Pfam; PF13807; GNVR; 1.
DR   Pfam; PF02706; Wzz; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01007; eps_fam; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane;
KW   Exopolysaccharide synthesis; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   CHAIN           1..719
FT                   /note="Tyrosine-protein kinase wzc"
FT                   /id="PRO_0000212356"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..423
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..719
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         568
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         707
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         709
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         710
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         712
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         714
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   719 AA;  79114 MW;  DEE6B32232658B1B CRC64;
     MTEKAKQSAA VTGSDEIDIG RLVGTVIEAR WWVLGTTAIF ALCAVIYTFF ATPIYSADAL
     VQIEQNAGNS LVQDINSALA NKPPASDAEI QLIRSRLVLG KTVDDLDLDI AVTKNTFPLF
     GAGWERLMGR HNEMVKVTTF TRPETMSGQI FTLKVLGDKR YQLVSDGGFS AQGVVGQPLN
     KDGVTMRVEA IDARPDTEFT VSKFSTLGMI NNLQNNLTVT ETGKDTGVLS LTFTGEDRDQ
     IREILNSITR NYLQQDIARK SEEAGKSLAF LAKQLPEVRS RLDVAENKLN AFRQDKDSVD
     LPLEAKAVLD SMVNIDAQLN ELTFKEAEIS KLFTKAHPAY RTLLEKRKAL EDEKAKLNGR
     VTAMPKTQQE IVRLTRDVES GQQVYMQLLN KQQELKITEA STVGDVRIVD PAITQPGVLK
     PKKALIILGS IILGLMLSIV GVLLRSLFNR GIESPQALEE HGISVYASIP LSEWQKARDS
     VKTIKGIKRY KQSQLLAVGN PTDLAIEAIR SLRTSLHFAM MQAQNNVLML TGVSPSIGKT
     FVCANLAAVI SQTHKRVLLI DCDMRKGYTH ELLGTNNVDG LSDILAGKGE IASCAKPTAI
     ANFDLIPRGQ VPPNPSELLM SERFGELIAW ASSRYDLVLI DTPPILAVTD AAIVGRHAGT
     TLMVARYAVN TLKEVETSLS RFDQNGIQVK GVILNSIFRR ATGYQDYGYY EYEYQSDSK
 
 
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