WZC_ECO57
ID WZC_ECO57 Reviewed; 720 AA.
AC Q8X7L9;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tyrosine-protein kinase wzc;
DE EC=2.7.10.-;
GN Name=wzc; OrderedLocusNames=Z3224, ECs2865;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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. Phosphorylates
CC udg (By similarity). {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-569 is phosphorylated in an
CC intramolecular reaction that generates a significant increase of
CC protein kinase activity. Then Tyr-708, Tyr-710, Tyr-711, Tyr-713 and
CC Tyr-715 are phosphorylated in an intermolecular Tyr-569-dependent
CC reaction (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the etk/wzc family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG57120.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB36288.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57120.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36288.1; ALT_INIT; Genomic_DNA.
DR PIR; A90987; A90987.
DR PIR; D85832; D85832.
DR RefSeq; NP_310892.2; NC_002695.1.
DR RefSeq; WP_000137171.1; NZ_SEKU01000011.1.
DR AlphaFoldDB; Q8X7L9; -.
DR BMRB; Q8X7L9; -.
DR SMR; Q8X7L9; -.
DR STRING; 155864.EDL933_3133; -.
DR EnsemblBacteria; AAG57120; AAG57120; Z3224.
DR EnsemblBacteria; BAB36288; BAB36288; ECs_2865.
DR GeneID; 912525; -.
DR KEGG; ece:Z3224; -.
DR KEGG; ecs:ECs_2865; -.
DR PATRIC; fig|386585.9.peg.2998; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_0_0_6; -.
DR OMA; QQIYIQL; -.
DR BRENDA; 2.7.10.1; 2026.
DR UniPathway; UPA00631; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..720
FT /note="Tyrosine-protein kinase wzc"
FT /id="PRO_0000212354"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..424
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 569
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 708
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 710
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 711
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 713
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 715
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 720 AA; 79395 MW; 44D538E5968C93FA CRC64;
MTEKVKQHAA PVTGSDEIDI GRLVGTVIEA RWWVIGITAV FALCAVVYTF FATPIYSADA
LVQIEQSSGN SLVQDIGSAL ANKPPASDAE IQLIRSRLVL GKTVDDLDLD IAVSKNTFPI
FGAGWDRLMG RQNETVKVTT FNRPKEMEDQ VFTLNVLDNK NYTLSSDGGF SARGQAGQIL
KKEGVTLMVE AIHARPGSEF TVTKYSTLGM INQLQNSLTV TENGKDAGVL SLTYTGEDRE
QIRDILNSIA RNYQEQNIER KSAEASKSLA FLAQQLPEVR SRLDVAENKL NAFRQDKDSV
DLPLEAKAVL DSMVNIDAQL NELTFKEAEI SKLYTKVHPA YRTLLEKRQA LEDEKAKLNG
RVTAMPKTQQ EIVRLTRDVE SGQQVYMQLL NKEQELKITE ASTVGDVRIV DPAITQPGVL
KPKKGLIILG AIILGLMLSI VGVLLRSLFN RGIESPQVLE EHGISVYASI PLSEWQKARD
SVKTIKGIKR YKQSQLLAVG NPTDLAIEAI RSLRTSLHFA MMQAQNNVLM MTGVSPSIGK
TFVCANLAAV ISQTNKRVLL IDCDMRKGYT HELLGTNNVN GLSEILIGQG DITTAAKPTS
IAKFDLIPRG QVPPNPSELL MSERFAELVN WASKNYDLVL IDTPPILAVT DAAIVGRHVG
TTLMVARYAV NTLKEVETSL SRFEQNGIPV KGVILNSIFR RASAYQDYGY YEYEYKSDAK
