(data stored in ACNUC7421 zone)

SWISSPROT: MRAY_SHESH

ID   MRAY_SHESH              Reviewed;         360 AA.
AC   A8FQ97;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   16-JAN-2019, entry version 70.
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=Ssed_0407;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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:
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:0000255|HAMAP-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; CP000821; ABV35020.1; -; Genomic_DNA.
DR   RefSeq; WP_012140757.1; NC_009831.1.
DR   SMR; A8FQ97; -.
DR   STRING; 425104.Ssed_0407; -.
DR   EnsemblBacteria; ABV35020; ABV35020; Ssed_0407.
DR   KEGG; sse:Ssed_0407; -.
DR   eggNOG; ENOG4105CPY; Bacteria.
DR   eggNOG; COG0472; LUCA.
DR   HOGENOM; HOG000275122; -.
DR   KO; K01000; -.
DR   OMA; LMSPLHH; -.
DR   OrthoDB; 1151822at2; -.
DR   BioCyc; SSED425104:G1G9Y-424-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002015; 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; A8FQ97.
DR   SWISS-2DPAGE; A8FQ97.
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Membrane; Peptidoglycan synthesis; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    360       Phospho-N-acetylmuramoyl-pentapeptide-
FT                                transferase.
FT                                /FTId=PRO_1000074563.
FT   TRANSMEM     21     41       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM     74     94       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM     97    117       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    135    155       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    168    188       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    199    219       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    236    256       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    263    283       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    288    308       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
FT   TRANSMEM    338    358       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00038}.
SQ   SEQUENCE   360 AA;  39805 MW;  733D7BF06F3E2A63 CRC64;
     MLVYLAEYLT QFYSGFNVFS YVTFRAILGL LTALIFSLWW GPKMIERLQM LQIGQVVRND
     GPESHFSKRG TPTMGGILIL AGVFISVLLW GDLASRYVWV VLFVLASFGL IGFIDDYRKV
     VRKDTKGLIA KWKYILQSLA ALVIAFYLYA SADLVGETQL VVPFFKDIMP QLGGFFIVLA
     YFTIVGSSNA VNLTDGLDGL AIMPTVMVAA AFALIAYLSG HVQFANYLHL PYLPGAGELV
     IVCTAIVGAG LGFLWFNTYP AQVFMGDVGS LALGAALGVI AVLVRQEILL VIMGGVFVME
     TVSVILQVGS YKLRGQRIFR MAPIHHHYEL KGWPEPRVIV RFWIISLFLV LLGLATLKLR
//

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