ETK_ECOLI
ID ETK_ECOLI Reviewed; 726 AA.
AC P38134; P75879;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tyrosine-protein kinase etk;
DE EC=2.7.10.-;
GN Name=etk; Synonyms=yccC; OrderedLocusNames=b0981, JW0964;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 628-726.
RX PubMed=2168385; DOI=10.1128/jb.172.9.5497-5500.1990;
RA Dassa J., Marck C., Boquet P.L.;
RT "The complete nucleotide sequence of the Escherichia coli gene appA reveals
RT significant homology between pH 2.5 acid phosphatase and glucose-1-
RT phosphatase.";
RL J. Bacteriol. 172:5497-5500(1990).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
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 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 -!- 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 -!- INTERACTION:
CC P38134; P38134: etk; NbExp=4; IntAct=EBI-562015, EBI-562015;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC Note=When the protein is overexpressed.
CC -!- PTM: Autophosphorylated. Dephosphorylated by etp.
CC -!- SIMILARITY: Belongs to the etk/wzc family. {ECO:0000305}.
CC -!- CAUTION: Seems to be expressed only in enteropathogenic E.coli strains;
CC in E.coli K12 / MG1655 and K12 / W3110 this operon is silenced by an
CC IS1D insertion in the promoter region. {ECO:0000305}.
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DR EMBL; U00096; AAC74066.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35746.1; -; Genomic_DNA.
DR EMBL; M58708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64839; C64839.
DR RefSeq; NP_415501.1; NC_000913.3.
DR RefSeq; WP_000208650.1; NZ_SSZK01000002.1.
DR PDB; 3CIO; X-ray; 2.50 A; A/D=452-726.
DR PDBsum; 3CIO; -.
DR AlphaFoldDB; P38134; -.
DR SMR; P38134; -.
DR BioGRID; 4261406; 391.
DR DIP; DIP-9526N; -.
DR IntAct; P38134; 2.
DR MINT; P38134; -.
DR STRING; 511145.b0981; -.
DR TCDB; 8.A.3.3.1; the cytoplasmic membrane-periplasmic auxiliary-1 (mpa1) protein with cytoplasmic (c) domain (mpa1-c or mpa1+c) family.
DR jPOST; P38134; -.
DR PaxDb; P38134; -.
DR PRIDE; P38134; -.
DR EnsemblBacteria; AAC74066; AAC74066; b0981.
DR EnsemblBacteria; BAA35746; BAA35746; BAA35746.
DR GeneID; 66670742; -.
DR GeneID; 947409; -.
DR KEGG; ecj:JW0964; -.
DR KEGG; eco:b0981; -.
DR PATRIC; fig|1411691.4.peg.1292; -.
DR EchoBASE; EB1773; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_0_0_6; -.
DR InParanoid; P38134; -.
DR OMA; VYGPKHP; -.
DR PhylomeDB; P38134; -.
DR BioCyc; EcoCyc:EG11826-MON; -.
DR BioCyc; MetaCyc:EG11826-MON; -.
DR BRENDA; 2.7.10.1; 2026.
DR EvolutionaryTrace; P38134; -.
DR PRO; PR:P38134; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA: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; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..726
FT /note="Tyrosine-protein kinase etk"
FT /id="PRO_0000212349"
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 726
FT /note="E -> EEN (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:3CIO"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 510..525
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 533..543
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 545..558
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:3CIO"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 575..578
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 597..600
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:3CIO"
FT TURN 605..608
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 621..625
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 628..640
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 642..647
FT /evidence="ECO:0007829|PDB:3CIO"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 665..672
FT /evidence="ECO:0007829|PDB:3CIO"
FT TURN 673..675
FT /evidence="ECO:0007829|PDB:3CIO"
FT HELIX 680..690
FT /evidence="ECO:0007829|PDB:3CIO"
FT STRAND 698..702
FT /evidence="ECO:0007829|PDB:3CIO"
SQ SEQUENCE 726 AA; 81242 MW; BAA060F59680DA22 CRC64;
MTTKNMNTPP GSTQENEIDL LRLVGELWDH RKFIISVTAL FTLIAVAYSL LSTPIYQADT
LVQVEQKQGN AILSGLSDMI PNSSPESAPE IQLLQSRMIL GKTIAELNLR DIVEQKYFPI
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
