MGT_STAES
ID MGT_STAES Reviewed; 269 AA.
AC Q8CNQ3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Monofunctional glycosyltransferase {ECO:0000255|HAMAP-Rule:MF_01434};
DE Short=MGT {ECO:0000255|HAMAP-Rule:MF_01434};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_01434};
DE AltName: Full=Peptidoglycan TGase {ECO:0000255|HAMAP-Rule:MF_01434};
GN Name=mgt {ECO:0000255|HAMAP-Rule:MF_01434}; OrderedLocusNames=SE_1559;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain
CC elongation using lipid-linked disaccharide-pentapeptide as the
CC substrate. {ECO:0000255|HAMAP-Rule:MF_01434}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01434};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01434}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01434};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01434}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC {ECO:0000255|HAMAP-Rule:MF_01434}.
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DR EMBL; AE015929; AAO05158.1; -; Genomic_DNA.
DR RefSeq; NP_765114.1; NC_004461.1.
DR RefSeq; WP_001830409.1; NZ_WBME01000010.1.
DR AlphaFoldDB; Q8CNQ3; -.
DR SMR; Q8CNQ3; -.
DR STRING; 176280.SE_1559; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAO05158; AAO05158; SE_1559.
DR GeneID; 50018341; -.
DR KEGG; sep:SE_1559; -.
DR PATRIC; fig|176280.10.peg.1523; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_1_2_9; -.
DR OMA; DERFYVH; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001411; 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:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
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 Gene3D; 1.10.3810.10; -; 1.
DR HAMAP; MF_01434; MGT; 1.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR022978; Monofunct_glyco_trans.
DR InterPro; IPR036950; PBP_transglycosylase.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Membrane; Peptidoglycan synthesis; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Monofunctional glycosyltransferase"
FT /id="PRO_0000083160"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01434"
SQ SEQUENCE 269 AA; 31393 MW; 7C776ABED906CCFF CRC64;
MKRSDKYTDD YIEQRYESQR PHYNTYYQPI GKPPKKKKSK RIFLKAIITI LILLIIFFGV
MYFISSRANV DDLKSIENKS DFVATENMPN YVKGAFISME DERFYKHHGF DIKGTTRALF
STISDRDVQG GSTITQQVVK NYYYDNERSF TRKIKELFVA RKVEKQYSKN QILSFYMNNI
YYGDNQYTVE GAANHYFGVT VDKNNSNMSQ ISVLQSAILA SKVNAPSVYD VNDMSNNYIN
RVKTNLEKMK QQNFISESQY QEAMSQLGN
