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PTPB2_ECOLI
ID   PTPB2_ECOLI             Reviewed;         157 AA.
AC   P42904; P76669; Q2M976;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=N-acetylgalactosamine-specific phosphotransferase enzyme IIB component 2;
DE            EC=2.7.1.-;
DE   AltName: Full=EIIB-Aga';
DE   AltName: Full=PTS system N-acetylgalactosamine-specific EIIB component 2;
GN   Name=agaV; Synonyms=yhaY; OrderedLocusNames=b3133, JW3102;
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   DISCUSSION OF SEQUENCE.
RX   PubMed=8932697; DOI=10.1099/13500872-142-2-231;
RA   Reizer J., Ramseier T.M., Reizer A., Charbit A., Saier M.H. Jr.;
RT   "Novel phosphotransferase genes revealed by bacterial genome sequencing: a
RT   gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in
RT   Escherichia coli.";
RL   Microbiology 142:231-250(1996).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active -transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. This
CC       system is involved in N-acetylgalactosamine transport.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57936.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA57936.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76167.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77180.1; -; Genomic_DNA.
DR   RefSeq; NP_417602.4; NC_000913.3.
DR   RefSeq; WP_001336162.1; NZ_LN832404.1.
DR   AlphaFoldDB; P42904; -.
DR   SMR; P42904; -.
DR   BioGRID; 4261156; 10.
DR   IntAct; P42904; 2.
DR   STRING; 511145.b3133; -.
DR   jPOST; P42904; -.
DR   PaxDb; P42904; -.
DR   PRIDE; P42904; -.
DR   EnsemblBacteria; AAC76167; AAC76167; b3133.
DR   EnsemblBacteria; BAE77180; BAE77180; BAE77180.
DR   GeneID; 947648; -.
DR   KEGG; ecj:JW3102; -.
DR   KEGG; eco:b3133; -.
DR   PATRIC; fig|1411691.4.peg.3598; -.
DR   EchoBASE; EB2617; -.
DR   eggNOG; COG3444; Bacteria.
DR   HOGENOM; CLU_116175_2_1_6; -.
DR   InParanoid; P42904; -.
DR   OMA; GQGQLWI; -.
DR   PhylomeDB; P42904; -.
DR   BioCyc; EcoCyc:G7632-MON; -.
DR   PRO; PR:P42904; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00001; PTS_IIB_man; 1.
DR   Gene3D; 3.40.35.10; -; 1.
DR   InterPro; IPR004720; PTS_IIB_sorbose-sp.
DR   InterPro; IPR036667; PTS_IIB_sorbose-sp_sf.
DR   InterPro; IPR018455; PTS_IIB_sorbose-sp_subgr.
DR   Pfam; PF03830; PTSIIB_sorb; 1.
DR   SUPFAM; SSF52728; SSF52728; 1.
DR   TIGRFAMs; TIGR00854; pts-sorbose; 1.
DR   PROSITE; PS51101; PTS_EIIB_TYPE_4; 1.
PE   4: Predicted;
KW   Cytoplasm; Kinase; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..157
FT                   /note="N-acetylgalactosamine-specific phosphotransferase
FT                   enzyme IIB component 2"
FT                   /id="PRO_0000186659"
FT   DOMAIN          1..157
FT                   /note="PTS EIIB type-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00424"
FT   ACT_SITE        15
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  17086 MW;  3DC895AD0CF15D41 CRC64;
     MPNIVLSRID ERLIHGQVGV QWVGFAGANL VLVANDEVAE DPVQQNLMEM VLAEGIAVRF
     WTLQKVIDNI HRAADRQKIL LVCKTPADFL TLVKGGVPVN RINVGNMHYA NGKQQIAKTV
     SVDAGDIAAF NDLKTAGVEC FVQGVPTEPA VDLFKLL
 
 
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