WZC_ECOLI
ID WZC_ECOLI Reviewed; 720 AA.
AC P76387; O08003; O08004; P71236;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Tyrosine-protein kinase wzc;
DE EC=2.7.10.-;
GN Name=wzc; OrderedLocusNames=b2060, JW2045;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8759852; DOI=10.1128/jb.178.16.4885-4893.1996;
RA Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R.;
RT "Organization of the Escherichia coli K-12 gene cluster responsible for
RT production of the extracellular polysaccharide colanic acid.";
RL J. Bacteriol. 178:4885-4893(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=10348860; DOI=10.1128/jb.181.11.3472-3477.1999;
RA Vincent C., Doublet P., Grangeasse C., Vaganay E., Cozzone A.J., Duclos B.;
RT "Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a
RT phosphotyrosine-protein phosphatase, Wzb.";
RL J. Bacteriol. 181:3472-3477(1999).
RN [6]
RP CHARACTERIZATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11090276; DOI=10.1006/jmbi.2000.4217;
RA Vincent C., Duclos B., Grangeasse C., Vaganay E., Riberty M., Cozzone A.J.,
RA Doublet P.;
RT "Relationship between exopolysaccharide production and protein-tyrosine
RT phosphorylation in Gram-negative bacteria.";
RL J. Mol. Biol. 304:311-321(2000).
RN [7]
RP CHARACTERIZATION, AND MUTAGENESIS.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11751920; DOI=10.1074/jbc.m110880200;
RA Grangeasse C., Doublet P., Cozzone A.J.;
RT "Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12
RT occurs through a two-step process.";
RL J. Biol. Chem. 277:7127-7135(2002).
RN [8]
RP PHOSPHORYLATION AT TYR-569; TYR-708; TYR-710; TYR-711; TYR-713 AND TYR-715,
RP AND FUNCTION.
RX PubMed=12851388; DOI=10.1074/jbc.m305134200;
RA Grangeasse C., Obadia B., Mijakovic I., Deutscher J., Cozzone A.J.,
RA Doublet P.;
RT "Autophosphorylation of the Escherichia coli protein kinase Wzc regulates
RT tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase.";
RL J. Biol. Chem. 278:39323-39329(2003).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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. {ECO:0000269|PubMed:12851388}.
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 -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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. {ECO:0000269|PubMed:12851388}.
CC -!- MISCELLANEOUS: Additional site-directed mutagenesis experiments
CC indicated that the tyrosine residues at positions 708, 710, 711, 713
CC and 715 are phosphorylation sites, whereas tyrosine at position 705 is
CC not.
CC -!- SIMILARITY: Belongs to the etk/wzc family. {ECO:0000305}.
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DR EMBL; U38473; AAC77835.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75121.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15913.1; -; Genomic_DNA.
DR PIR; C64972; C64972.
DR RefSeq; NP_416564.4; NC_000913.3.
DR RefSeq; WP_000137196.1; NZ_LN832404.1.
DR PDB; 3LA6; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=447-720.
DR PDBsum; 3LA6; -.
DR AlphaFoldDB; P76387; -.
DR BMRB; P76387; -.
DR SMR; P76387; -.
DR BioGRID; 4262960; 336.
DR DIP; DIP-28075N; -.
DR IntAct; P76387; 5.
DR MINT; P76387; -.
DR STRING; 511145.b2060; -.
DR TCDB; 8.A.3.3.2; the cytoplasmic membrane-periplasmic auxiliary-1 (mpa1) protein with cytoplasmic (c) domain (mpa1-c or mpa1+c) family.
DR iPTMnet; P76387; -.
DR PaxDb; P76387; -.
DR PRIDE; P76387; -.
DR EnsemblBacteria; AAC75121; AAC75121; b2060.
DR EnsemblBacteria; BAA15913; BAA15913; BAA15913.
DR GeneID; 946567; -.
DR KEGG; ecj:JW2045; -.
DR KEGG; eco:b2060; -.
DR PATRIC; fig|511145.12.peg.2137; -.
DR EchoBASE; EB3338; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_0_0_6; -.
DR InParanoid; P76387; -.
DR OMA; QQIYIQL; -.
DR PhylomeDB; P76387; -.
DR BioCyc; EcoCyc:G7105-MON; -.
DR BioCyc; MetaCyc:G7105-MON; -.
DR BRENDA; 2.7.10.1; 2026.
DR UniPathway; UPA00631; -.
DR PRO; PR:P76387; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:EcoCyc.
DR GO; GO:0009242; P:colanic acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000212353"
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:0000305|PubMed:12851388"
FT MOD_RES 708
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12851388"
FT MOD_RES 710
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12851388"
FT MOD_RES 711
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12851388"
FT MOD_RES 713
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12851388"
FT MOD_RES 715
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:12851388"
FT MUTAGEN 467
FT /note="Y->F: No loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11751920"
FT MUTAGEN 491
FT /note="Y->F: No loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11751920"
FT MUTAGEN 540
FT /note="K->M: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11751920"
FT MUTAGEN 569
FT /note="Y->F: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11751920"
FT MUTAGEN 636
FT /note="Y->F: No loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11751920"
FT MUTAGEN 668
FT /note="Y->F: No loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11751920"
FT HELIX 456..460
FT /evidence="ECO:0007829|PDB:3LA6"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:3LA6"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 474..478
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 505..520
FT /evidence="ECO:0007829|PDB:3LA6"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:3LA6"
FT STRAND 528..539
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 540..552
FT /evidence="ECO:0007829|PDB:3LA6"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:3LA6"
FT STRAND 558..562
FT /evidence="ECO:0007829|PDB:3LA6"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 570..574
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 582..587
FT /evidence="ECO:0007829|PDB:3LA6"
FT TURN 592..595
FT /evidence="ECO:0007829|PDB:3LA6"
FT STRAND 604..607
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 616..620
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 623..635
FT /evidence="ECO:0007829|PDB:3LA6"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:3LA6"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 651..655
FT /evidence="ECO:0007829|PDB:3LA6"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:3LA6"
FT STRAND 660..667
FT /evidence="ECO:0007829|PDB:3LA6"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:3LA6"
FT HELIX 673..685
FT /evidence="ECO:0007829|PDB:3LA6"
FT STRAND 692..698
FT /evidence="ECO:0007829|PDB:3LA6"
SQ SEQUENCE 720 AA; 79343 MW; 8F61017B5ECFFB45 CRC64;
MTEKVKQHAA PVTGSDEIDI GRLVGTVIEA RWWVIGITTV FALCAVVYTF FATPIYSADA
LVQIEQNSGN SLVQDIGSAL ANKPPASDAE IQLIRSRLVL GKTVDDLDLD IAVSKNTFPI
FGAGWDRLMG RQNETVKVTT FNRPKEMADQ VFTLNVLDNK NYTLSSDGGF SARGQAGQML
KKEGVTLMVE AIHASPGSEF 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
