(data stored in ACNUC7421 zone)

SWISSPROT: MURG_SHESH

ID   MURG_SHESH              Reviewed;         365 AA.
AC   A8FQA0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000255|HAMAP-Rule:MF_00033};
DE            EC=2.4.1.227 {ECO:0000255|HAMAP-Rule:MF_00033};
DE   AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000255|HAMAP-Rule:MF_00033};
GN   Name=murG {ECO:0000255|HAMAP-Rule:MF_00033};
GN   OrderedLocusNames=Ssed_0410;
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: Cell wall formation. Catalyzes the transfer of a GlcNAc
CC       subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid
CC       intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-
CC       (pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-
CC       Rule:MF_00033}.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-
CC       gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP +
CC       GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC       diphosphoundecaprenol. {ECO:0000255|HAMAP-Rule:MF_00033}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00033}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00033}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00033}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00033}.
DR   EMBL; CP000821; ABV35023.1; -; Genomic_DNA.
DR   RefSeq; WP_012140760.1; NC_009831.1.
DR   ProteinModelPortal; A8FQA0; -.
DR   SMR; A8FQA0; -.
DR   STRING; 425104.Ssed_0410; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   EnsemblBacteria; ABV35023; ABV35023; Ssed_0410.
DR   KEGG; sse:Ssed_0410; -.
DR   eggNOG; ENOG4105DVQ; Bacteria.
DR   eggNOG; COG0707; LUCA.
DR   HOGENOM; HOG000218321; -.
DR   KO; K02563; -.
DR   OMA; HQTKNAM; -.
DR   OrthoDB; POG091H02FX; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051991; F:UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:0030259; P:lipid glycosylation; IEA:InterPro.
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; cd03785; GT1_MurG; 1.
DR   HAMAP; MF_00033; MurG; 1.
DR   InterPro; IPR006009; GlcNAc_MurG.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   TIGRFAMs; TIGR01133; murG; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQA0.
DR   SWISS-2DPAGE; A8FQA0.
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Glycosyltransferase; Membrane; Peptidoglycan synthesis; Transferase.
FT   CHAIN         1    365       UDP-N-acetylglucosamine--N-acetylmuramyl-
FT                                (pentapeptide) pyrophosphoryl-
FT                                undecaprenol N-acetylglucosamine
FT                                transferase.
FT                                /FTId=PRO_1000074472.
SQ   SEQUENCE   365 AA;  38782 MW;  14110E4532C7B393 CRC64;
     MTTVNTDKRI LIMAGGTGGH VFPALAVAKY LCQQGWQVRW LGTAERMEAR LVPQHGFDID
     FIDIKGVRGN GLLRKLAAPF KVIRSIMQAQ AVIKEFKPDV VLGMGGFASG PGGVAARLSG
     LPLVLHEQNA IPGMTNKILA RIASQVLCAF EDTFDNVEAE VVGNPIREEL IALGDSNVDP
     VTDDALKVLV VGGSLGAKVF NDLMPSVTAA VSKTHSITVW HQVGKGNLQG VKAEYQHLGQ
     DGSVNVAEFI DDMEAAYRWA DVVLCRSGAL TVSEVAAVGL PSLLVPYPHA VDDHQTKNAQ
     VLVQAGGAFL LPQTILDANK LIGKLQILAS DRNELAQMGL RAKSAAVLDA TQKVASVCIR
     LAGKD
//

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