ID   ETK_ECO57               Reviewed;         726 AA.
AC   Q8XC28;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Tyrosine-protein kinase etk;
DE            EC=2.7.10.-;
GN   Name=etk; OrderedLocusNames=Z1398, ECs1137;
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   -!- 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   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. Dephosphorylated by etp (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the etk/wzc family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG55529.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34560.1; -; Genomic_DNA.
DR   PIR; A90771; A90771.
DR   PIR; E85633; E85633.
DR   RefSeq; NP_309164.1; NC_002695.1.
DR   RefSeq; WP_000208668.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XC28; -.
DR   SMR; Q8XC28; -.
DR   STRING; 155864.EDL933_1319; -.
DR   EnsemblBacteria; AAG55529; AAG55529; Z1398.
DR   EnsemblBacteria; BAB34560; BAB34560; ECs_1137.
DR   GeneID; 912586; -.
DR   KEGG; ece:Z1398; -.
DR   KEGG; ecs:ECs_1137; -.
DR   PATRIC; fig|386585.9.peg.1253; -.
DR   eggNOG; COG0489; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   HOGENOM; CLU_009912_0_0_6; -.
DR   OMA; VYGPKHP; -.
DR   BRENDA; 2.7.10.1; 2026.
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; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   CHAIN           1..726
FT                   /note="Tyrosine-protein kinase etk"
FT                   /id="PRO_0000212351"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..424
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        446..726
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   726 AA;  81260 MW;  7EEA1912097118DC CRC64;
     MTTKNMNTPP GSTQENEIDL LRLVGELWDH RKFIISVTAL FTLIAVAYSL LSTPIYQADT
     LVQVEQKQGN AILSGLSDMI PNSSPESAPE IQLLQSRMIL GKTIAELNLR DMVEQKYFPI
     VGRGWARLTK EKPGELAISW MHIPQLNGQD QQLTLTVGEN GHYTLEGEEF TVNGMVGQRL
     EKDGVALTIA DIKAKPGTQF VLSQRTELEA INALQETFTV SERSKESGML ELTMTGDDPQ
     LITRILNSIA NNYLQQNIAR QAAQDSQSLE FLQRQLPEVR SELDQAEEKL NVYRQQRDSV
     DLNLEAKAVL EQIVNVDNQL NELTFREAEI SQLYKKDHPT YRALLEKRQT LEQERKRLNK
     RVSAMPSTQQ EVLRLSRDVE AGRAVYLQLL NRQQELSISK SSAIGNVRII DPAVTQPQPV
     KPKKALNVVL GFILGLFISV GAVLARAMLR RGVEAPEQLE EHGISVYATI PMSEWLDKRT
     RLRKKNLFSN QQRHRTKNIP FLAVDNPADS AVEAVRALRT SLHFAMMETE NNILMITGAT
     PDSGKTFVSS TLAAVIAQSD QKVLFIDADL RRGYSHNLFT VSNEHGLSEY LAGKDELNKV
     IQHFGKGGFD VITRGQVPPN PSELLMRDRM RQLLEWANDH YDLVIVDTPP MLAVSDAAVV
     GRSVGTSLLV ARFGLNTAKE VSLSMQRLEQ AGVNIKGAIL NGVIKRASTA YSYGYNYYGY
     SYSEKE