WZC_SALTI
ID WZC_SALTI Reviewed; 719 AA.
AC Q8Z5G6;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tyrosine-protein kinase wzc;
DE EC=2.7.10.-;
GN Name=wzc; OrderedLocusNames=STY2329, t0756;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD02479.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68449.1; -; Genomic_DNA.
DR RefSeq; NP_456662.1; NC_003198.1.
DR RefSeq; WP_000137223.1; NZ_WSUR01000002.1.
DR AlphaFoldDB; Q8Z5G6; -.
DR SMR; Q8Z5G6; -.
DR STRING; 220341.16503343; -.
DR EnsemblBacteria; AAO68449; AAO68449; t0756.
DR KEGG; stt:t0756; -.
DR KEGG; sty:STY2329; -.
DR PATRIC; fig|220341.7.peg.2350; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_0_0_6; -.
DR OMA; QQIYIQL; -.
DR UniPathway; UPA00631; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
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; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT CHAIN 1..719
FT /note="Tyrosine-protein kinase wzc"
FT /id="PRO_0000212355"
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; 79187 MW; 832E016D7F09BDFE CRC64;
MTEKVKQSAA VTGSDEIDIG RLVGTVIEAR WWVLGTTAIF ALCAVIYTFF ATPIYSADAL
VQIEQNAGNS LVQDINSALA NKPPASDAEI QLIRSRLVLG KTVDDLDLDI AVTKNTFPLF
GAGWERLMGR HNEMVKVTTF TRPETMSGQI FTLKVLGDKR YQLVSDGGFS AQGVVGQPLN
KDGVTMRVEA IDARPDTEFT VSKFSTLGMI NNLQNNLTVT ETGKDTGVLN LTFTGEDRDQ
IRDILNSITR NYLQQDIAWK SEEAGKSLAF LAKQLPEVRS RLDVAENKLN AFRQDKDSVD
LPLEAKAVLD SMVNIDAQLN ELTFKEAEIS KLFTKAHPAY RTLLEKRKGL EDKKAKLNGR
VTAMPKTQQE IVRLTRDVES GQQVYMQLLN KQQELKITEA STVGNVRIVD PAITQPGVLK
PKKALIILGS IILGLMLSIV GVLLRSLFNR GIESPQALEE HGISVYASIP LSEWQKARDS
VKTIKGIKRY KQSQLLAVGN PTDLAIEAIR SLRTSLHFAM MQAQNNVLML TGVSSSIGKT
FVCANLAAVI SQTHKRVLLI DCDMRKGYTH ELLGTNNVDG LSDILAGKGE IASCAKPTAI
ANFDLIPRGQ VPPNPSELLM SERFGELIAW ASSRYDLVLI DTPPILAVTD AAIVGRHVGT
TLMVARYAVN TLKEVETSLS RFDQNGIQVK GVILNSIFRR ATGYQDYGYY EYEYQSDSK
