ID   ETK_ECO27               Reviewed;         726 AA.
AC   P58764; B7UN59;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Tyrosine-protein kinase etk;
DE            EC=2.7.10.-;
GN   Name=etk; OrderedLocusNames=E2348C_0966;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17, AND
RP   CHARACTERIZATION.
RX   PubMed=10369665; DOI=10.1093/emboj/18.12.3241;
RA   Ilan O.A., Bloch Y., Frankel G., Ullrich H., Geider K., Rosenshine I.;
RT   "Protein tyrosine kinases in bacterial pathogens are associated with
RT   virulence and production of exopolysaccharide.";
RL   EMBO J. 18:3241-3248(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; Multi-pass membrane protein.
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; AJ238695; CAB43868.1; -; Genomic_DNA.
DR   EMBL; FM180568; CAS08514.1; -; Genomic_DNA.
DR   RefSeq; WP_000208660.1; NC_011601.1.
DR   AlphaFoldDB; P58764; -.
DR   SMR; P58764; -.
DR   EnsemblBacteria; CAS08514; CAS08514; E2348C_0966.
DR   KEGG; ecg:E2348C_0966; -.
DR   HOGENOM; CLU_009912_0_0_6; -.
DR   OMA; VYGPKHP; -.
DR   BRENDA; 2.7.10.1; 2026.
DR   BRENDA; 2.7.10.2; 2026.
DR   Proteomes; UP000008205; 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   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   CHAIN           1..726
FT                   /note="Tyrosine-protein kinase etk"
FT                   /id="PRO_0000212350"
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"
FT   CONFLICT        92
FT                   /note="Q -> L (in Ref. 1; CAB43868)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   726 AA;  81098 MW;  961FBC1596801E02 CRC64;
     MTTKNMNTPP GSTQENEIDL LRLVGELWDH RKFIISVTAL FTLIAVAYSL LSTPIYQADT
     LVQVEQKQGN AILSGLSDMI PNSSPESAPE IQLLQSRMIL GKTIAELNLR DIVEQKYFPI
     VGRGWARLTK EKPGELAISW MHIPQLNGQD QQLTLTVGEN GHYTLEGEGF TVNGMVGQRL
     EKDGVALTIA DIKAKPGTQF VLSQRTELEA INALQGTFTV 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