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PTYBC_ECOUT
ID   PTYBC_ECOUT             Reviewed;         474 AA.
AC   Q1R8U3;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=PTS system N-acetylmuramic acid-specific EIIBC component {ECO:0000250|UniProtKB:P77272};
DE   AltName: Full=EIIBC-MurNAc {ECO:0000250|UniProtKB:P77272};
DE   Includes:
DE     RecName: Full=N-acetylmuramic acid-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P77272};
DE              EC=2.7.1.192 {ECO:0000250|UniProtKB:P77272};
DE     AltName: Full=PTS system N-acetylmuramic acid-specific EIIB component {ECO:0000250|UniProtKB:P77272};
DE   Includes:
DE     RecName: Full=N-acetylmuramic acid permease IIC component {ECO:0000250|UniProtKB:P77272};
DE     AltName: Full=PTS system N-acetylmuramic acid-specific EIIC component {ECO:0000250|UniProtKB:P77272};
GN   Name=murP; OrderedLocusNames=UTI89_C2761;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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-acetylmuramic acid (MurNAc) transport, yielding
CC       cytoplasmic MurNAc-6-P. Is also able to take up anhydro-N-acetylmuramic
CC       acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably
CC       because of the 1,6-anhydro ring. {ECO:0000250|UniProtKB:P77272}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-beta-D-
CC         muramate(out) = L-histidyl-[protein] + N-acetyl-beta-D-muramate 6-
CC         phosphate(in); Xref=Rhea:RHEA:33399, Rhea:RHEA-COMP:9745, Rhea:RHEA-
CC         COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:58721, ChEBI:CHEBI:64837,
CC         ChEBI:CHEBI:64848; EC=2.7.1.192;
CC         Evidence={ECO:0000250|UniProtKB:P77272};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}.
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       {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC       contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}.
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DR   EMBL; CP000243; ABE08221.1; -; Genomic_DNA.
DR   RefSeq; WP_001040463.1; NC_007946.1.
DR   AlphaFoldDB; Q1R8U3; -.
DR   SMR; Q1R8U3; -.
DR   EnsemblBacteria; ABE08221; ABE08221; UTI89_C2761.
DR   KEGG; eci:UTI89_C2761; -.
DR   HOGENOM; CLU_012312_2_0_6; -.
DR   OMA; VAHCMTR; -.
DR   Proteomes; UP000001952; 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: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; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; -; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; SSF55604; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..474
FT                   /note="PTS system N-acetylmuramic acid-specific EIIBC
FT                   component"
FT                   /id="PRO_0000248955"
FT   TOPO_DOM        1..123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        145..157
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        179..180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        202..217
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        239..260
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        282..301
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        323..334
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        356..368
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        390..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        415..440
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TOPO_DOM        462..474
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..89
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   DOMAIN          115..474
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   ACT_SITE        29
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   474 AA;  49815 MW;  76E0204B5F0B8AC7 CRC64;
     MAKEISSELL NTILTRVGGP GNIASCGNCM TRLRLGVHDS SLVDPDIKTL EGVKGVILTS
     DQVQVVFGPG KAHRAAKAMS ELLGEAPVQD AAEIAAQNKR QLKARQTSGV QQFLAKFATI
     FTPLIPGFIA AGLLLGIATL IATVMHVTAD AQGTLPDALN FMKVFSKGLF TFLVILVGYN
     AAQAFGGTGV NGAIIAALFL LGYNPTATTG YYAGFHDFFG LPIDPRGNII GVLIAAWACA
     RIEGMVRRFM PDDLDMLLTS LITLLITATL AYLIIMPLGG WLFEGMSWLF MHLNSNPLGC
     AVLAGLFLIA VVFGVHQGFI PVYLALMDSQ GFNSLFPILS MAGAGQVGAA LALYWRAQPH
     SALRSQVRGA IIPGLLGVGE PLIYGVTLPR MKPFVTACLG GAAGGLFIGL IAWWGLPMGL
     NSAFGPSGLV ALPLMTSAQG ILPAMAVYAG GILVAWVSGF IFTTLFGCRN VNLD
 
 
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