YNBD_ECOLI
ID YNBD_ECOLI Reviewed; 430 AA.
AC P76093; Q2MBC4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Uncharacterized protein YnbD;
GN Name=ynbD; OrderedLocusNames=b1411, JW1408;
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 / 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-430.
RC STRAIN=K12;
RA Kitakawa M., Kasai H., Baba T., Honjo A., Isono K.;
RT "Nucleotide sequence of the replication terminus region of Escherichia
RT coli.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- INTERACTION:
CC P76093; P17169: glmS; NbExp=4; IntAct=EBI-551038, EBI-551022;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC74493.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76432.1; -; Genomic_DNA.
DR EMBL; D85081; BAA25407.1; -; Genomic_DNA.
DR PIR; F64892; F64892.
DR RefSeq; NP_415929.1; NC_000913.3.
DR RefSeq; WP_001375099.1; NZ_JACEFS010000028.1.
DR AlphaFoldDB; P76093; -.
DR SMR; P76093; -.
DR BioGRID; 4263024; 21.
DR BioGRID; 850347; 1.
DR DIP; DIP-12745N; -.
DR IntAct; P76093; 2.
DR STRING; 511145.b1411; -.
DR PaxDb; P76093; -.
DR PRIDE; P76093; -.
DR EnsemblBacteria; AAC74493; AAC74493; b1411.
DR EnsemblBacteria; BAE76432; BAE76432; BAE76432.
DR GeneID; 945985; -.
DR KEGG; ecj:JW1408; -.
DR KEGG; eco:b1411; -.
DR PATRIC; fig|511145.12.peg.1474; -.
DR EchoBASE; EB3514; -.
DR eggNOG; COG0671; Bacteria.
DR eggNOG; COG2453; Bacteria.
DR HOGENOM; CLU_031173_0_0_6; -.
DR InParanoid; P76093; -.
DR OMA; QHHFIDI; -.
DR PhylomeDB; P76093; -.
DR BioCyc; EcoCyc:G6730-MON; -.
DR PRO; PR:P76093; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protein phosphatase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..430
FT /note="Uncharacterized protein YnbD"
FT /id="PRO_0000094929"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 297..430
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 376
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 430 AA; 49563 MW; 7707978DD3F05EB8 CRC64;
MLQGAGWLLL LAPFFFFTYG SLNQFTAVQD LNSHDIPSQV FGWETAIPFL PWTIVPYWSL
DLLYGFSLFV CSTTFEQRRL VHRLILATVM ACCGFLLYPL KFSFIRPEVS GVTGWLFSQL
ELFDLPYNQS PSLHIILCWL LWRHFRQHLA ERWRKVCGGW FLLIAISTLT TWQHHFIDVI
TGLAVGMLID WMVPVDRRWN YQKPDQRRIK IALPYVVGAG SCIVLMELMM MIQLWWSVWL
CWPVLSLLII GRGYGGLGAI TTGKDSQGKL PPAVYWLTLP CRIGMWLSMR WFCRRLEPVS
KMTAGVYLGA FPRHIPAQNA VLDVTFEFPR GRATKDRLYF CVPMLDLVVP EEGELRQAVA
MLETLREEQG SVLVHCALGL SRSALVVAAW LLCYGHCKTV NEAISYIRAR RPQIVLTDEH
KAMLRLWENR