(data stored in ACNUC7421 zone)

SWISSPROT: MRAY_ECODH

ID   MRAY_ECODH              Reviewed;         360 AA.
AC   B1XC64;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 64.
DE   RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000255|HAMAP-Rule:MF_00038};
DE            EC=2.7.8.13 {ECO:0000255|HAMAP-Rule:MF_00038};
DE   AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038};
GN   Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038};
GN   OrderedLocusNames=ECDH10B_0069;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: First step of the lipid cycle reactions in the
CC       biosynthesis of the cell wall peptidoglycan. {ECO:0000255|HAMAP-
CC       Rule:MF_00038}.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00038}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00038}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00038}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}.
DR   EMBL; CP000948; ACB01268.1; -; Genomic_DNA.
DR   RefSeq; WP_000964131.1; NC_010473.1.
DR   ProteinModelPortal; B1XC64; -.
DR   SMR; B1XC64; -.
DR   EnsemblBacteria; ACB01268; ACB01268; ECDH10B_0069.
DR   KEGG; ecd:ECDH10B_0069; -.
DR   eggNOG; ENOG4105CPY; Bacteria.
DR   eggNOG; COG0472; LUCA.
DR   HOGENOM; HOG000275122; -.
DR   KO; K01000; -.
DR   OMA; LMSPLHH; -.
DR   UniPathway; UPA00219; -.
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; B1XC64.
DR   SWISS-2DPAGE; B1XC64.
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Membrane;
KW   Peptidoglycan synthesis; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    360       Phospho-N-acetylmuramoyl-pentapeptide-
FT                                transferase.
FT                                /FTId=PRO_1000090624.
FT   TOPO_DOM      1     25       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM     26     46       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM     47     71       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM     72     92       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM     93     93       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM     94    114       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM    115    131       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    132    152       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM    153    167       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    168    188       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM    189    198       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    199    219       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM    220    235       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    236    256       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM    257    262       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    263    283       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM    284    287       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    288    308       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM    309    337       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    338    358       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TOPO_DOM    359    360       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
SQ   SEQUENCE   360 AA;  39875 MW;  F3550AFA3CD636AE CRC64;
     MLVWLAEHLV KYYSGFNVFS YLTFRAIVSL LTALFISLWM GPRMIAHLQK LSFGQVVRND
     GPESHFSKRG TPTMGGIMIL TAIVISVLLW AYPSNPYVWC VLVVLVGYGV IGFVDDYRKV
     VRKDTKGLIA RWKYFWMSVI ALGVAFALYL AGKDTPATQL VVPFFKDVMP QLGLFYILLA
     YFVIVGTGNA VNLTDGLDGL AIMPTVFVAG GFALVAWATG NMNFASYLHI PYLRHAGELV
     IVCTAIVGAG LGFLWFNTYP AQVFMGDVGS LALGGALGII AVLLRQEFLL VIMGGVFVVE
     TLSVILQVGS FKLRGQRIFR MAPIHHHYEL KGWPEPRVIV RFWIISLMLV LIGLATLKVR
//

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