ID F4TCL2_ECOLX Unreviewed; 726 AA.
AC F4TCL2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Tyrosine-protein kinase etk {ECO:0000313|EMBL:EGI22342.1};
GN ORFNames=ECJG_00436 {ECO:0000313|EMBL:EGI22342.1};
OS Escherichia coli M718.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656419 {ECO:0000313|EMBL:EGI22342.1, ECO:0000313|Proteomes:UP000002790};
RN [1] {ECO:0000313|EMBL:EGI22342.1, ECO:0000313|Proteomes:UP000002790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M718 {ECO:0000313|EMBL:EGI22342.1,
RC ECO:0000313|Proteomes:UP000002790};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli M718.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001074};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the etk/wzc family.
CC {ECO:0000256|ARBA:ARBA00008883}.
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DR EMBL; GL884111; EGI22342.1; -; Genomic_DNA.
DR RefSeq; WP_000208663.1; NZ_GL884111.1.
DR AlphaFoldDB; F4TCL2; -.
DR HOGENOM; CLU_009912_0_0_6; -.
DR Proteomes; UP000002790; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05387; BY-kinase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR032807; GNVR.
DR InterPro; IPR003856; LPS_length_determ_N_term.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005702; Wzc-like_C.
DR NCBIfam; TIGR01007; eps_fam; 1.
DR PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR Pfam; PF13614; AAA_31; 1.
DR Pfam; PF13807; GNVR; 1.
DR Pfam; PF02706; Wzz; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGI22342.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..107
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 368..448
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 543..654
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 269..303
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 726 AA; 81232 MW; 7EEA1E1BAE85DE47 CRC64;
MTTKNMNTPP GSTQENEIDL LRLVGELWDH RKFIISVTAL FTLIAVAYSL LSTPIYQADT
LVQVEQKQGN AILSGLSDMI PNSSPESAPE IQLLQSRMIL GKTIAELNLR DMVEQKYFPI
VGRGWARLTK EKPGELAISW MHIPQLNGQD QQLTLTVGEN GHYTLEGEEF TANGMVGQRL
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
//
