(data stored in ACNUC10821 zone)

SWISSPROT: C8U1F9_ECO10

ID   C8U1F9_ECO10            Unreviewed;       360 AA.
AC   C8U1F9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-DEC-2018, entry version 55.
DE   RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000256|HAMAP-Rule:MF_00038};
DE            EC=2.7.8.13 {ECO:0000256|HAMAP-Rule:MF_00038};
DE   AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00038};
GN   Name=mraY {ECO:0000256|HAMAP-Rule:MF_00038,
GN   ECO:0000313|EMBL:BAI28967.1};
GN   OrderedLocusNames=ECO103_0089 {ECO:0000313|EMBL:BAI28967.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28967.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28967.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: First step of the lipid cycle reactions in the
CC       biosynthesis of the cell wall peptidoglycan. {ECO:0000256|HAMAP-
CC       Rule:MF_00038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-
CC         alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC         alanine = Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC         diphospho-di-trans,octa-cis-undecaprenol + UMP;
CC         Xref=Rhea:RHEA:21920, ChEBI:CHEBI:57865, ChEBI:CHEBI:60032,
CC         ChEBI:CHEBI:60392, ChEBI:CHEBI:70758; EC=2.7.8.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00038};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00038}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00038}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00038}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00038}.
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DR   EMBL; AP010958; BAI28967.1; -; Genomic_DNA.
DR   RefSeq; WP_000964126.1; NC_013353.1.
DR   EnsemblBacteria; BAI28967; BAI28967; ECO103_0089.
DR   KEGG; eoh:ECO103_0089; -.
DR   HOGENOM; HOG000275122; -.
DR   KO; K01000; -.
DR   OMA; LMSPLHH; -.
DR   BioCyc; ECOL585395:ECO103_RS00450-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000959; 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-UniRule.
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-UniRule.
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; C8U1F9.
DR   SWISS-2DPAGE; C8U1F9.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00038,
KW   ECO:0000313|EMBL:BAI28967.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00038}.
FT   TRANSMEM     20     40       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM     73     90       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM     96    114       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    134    152       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    172    193       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    200    219       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    239    256       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    263    284       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    290    311       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
FT   TRANSMEM    338    357       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00038}.
SQ   SEQUENCE   360 AA;  39889 MW;  6639B2DF5D2A83CF CRC64;
     MLVWLAEHLV KYYSGFNVFS YLTFRAIVSL LTALFISLWM GPRMIAHLQK LSFGQVVRND
     GPESHFSKRG TPTMGGIMIL TAIVISVLLW AYPSNPYVWC VLVVLVGYGV IGFVDDYRKV
     VRKDTKGLIA RWKYFWMSVI ALGIAFALYL 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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