(data stored in ACNUC7421 zone)

SWISSPROT: MRAY_ECO57

ID   MRAY_ECO57              Reviewed;         360 AA.
AC   P64258; Q8X9Z0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   05-JUL-2017, entry version 92.
DE   RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase;
DE            EC=2.7.8.13;
DE   AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase;
GN   Name=mraY; OrderedLocusNames=Z0097, ECs0091;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: First step of the lipid cycle reactions in the
CC       biosynthesis of the cell wall peptidoglycan. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-
CC       D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-
CC       Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000305}.
DR   EMBL; AE005174; AAG54391.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33514.1; -; Genomic_DNA.
DR   PIR; C85491; C85491.
DR   PIR; C90640; C90640.
DR   RefSeq; NP_308118.1; NC_002695.1.
DR   RefSeq; WP_000964134.1; NZ_MWVM01000012.1.
DR   STRING; 155864.Z0097; -.
DR   EnsemblBacteria; AAG54391; AAG54391; Z0097.
DR   EnsemblBacteria; BAB33514; BAB33514; BAB33514.
DR   GeneID; 913542; -.
DR   KEGG; ece:Z0097; -.
DR   KEGG; ecs:ECs0091; -.
DR   PATRIC; fig|386585.9.peg.191; -.
DR   eggNOG; ENOG4105CPY; Bacteria.
DR   eggNOG; COG0472; LUCA.
DR   HOGENOM; HOG000275122; -.
DR   KO; K01000; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051992; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd06852; GT_MraY; 1.
DR   HAMAP; MF_00038; MraY; 1.
DR   InterPro; IPR000715; Glycosyl_transferase_4.
DR   InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase.
DR   InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR   PANTHER; PTHR22926; PTHR22926; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
DR   Pfam; PF10555; MraY_sig1; 1.
DR   TIGRFAMs; TIGR00445; mraY; 1.
DR   PROSITE; PS01347; MRAY_1; 1.
DR   PROSITE; PS01348; MRAY_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; P64258.
DR   SWISS-2DPAGE; P64258.
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Membrane; Peptidoglycan synthesis; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    360       Phospho-N-acetylmuramoyl-pentapeptide-
FT                                transferase.
FT                                /FTId=PRO_0000108822.
FT   TOPO_DOM      1     25       Periplasmic. {ECO:0000255}.
FT   TRANSMEM     26     46       Helical. {ECO:0000255}.
FT   TOPO_DOM     47     71       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     72     92       Helical. {ECO:0000255}.
FT   TOPO_DOM     93     93       Periplasmic. {ECO:0000255}.
FT   TRANSMEM     94    114       Helical. {ECO:0000255}.
FT   TOPO_DOM    115    131       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    132    152       Helical. {ECO:0000255}.
FT   TOPO_DOM    153    167       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    168    188       Helical. {ECO:0000255}.
FT   TOPO_DOM    189    198       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    199    219       Helical. {ECO:0000255}.
FT   TOPO_DOM    220    235       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    236    256       Helical. {ECO:0000255}.
FT   TOPO_DOM    257    262       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    263    283       Helical. {ECO:0000255}.
FT   TOPO_DOM    284    287       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    288    308       Helical. {ECO:0000255}.
FT   TOPO_DOM    309    337       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    338    358       Helical. {ECO:0000255}.
FT   TOPO_DOM    359    360       Periplasmic. {ECO:0000255}.
SQ   SEQUENCE   360 AA;  39903 MW;  922AB374BC9E8F2E CRC64;
     MLVWLAEHLV KYYSGFNVFS YLTFRAIVSL LTALFISLWM GPRMIAHLQK LSFGQVVRND
     GPESHFSKRG TPTMGGIMIL TAIVISVLLW AYPSNPYVWC VLVVLVGYGV IGFVDDYRKV
     VRKDTKGLIA RWKYFWMSVI ALGVAFALYL VGKDTPATQL VVPFFKDVMP QLGLFYILLA
     YFVIVGTGNA VNLTDGLDGL AIMPTVFVAG GFALVAWATG NMNFASYLHI PYLRHAGELV
     IVCTAIVGAG LGFLWFNTYP AQVFMGDVGS LALGGALGII AVLLRQEFLL VIMGGVFVVE
     TLSVILQVGS FKLRGQRIFR MAPIHHHYEL KGWPEPRVIV RFWIISLMLV LIGLATLKVR
//

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