ID   MGT_STAAB               Reviewed;         269 AA.
AC   Q2YU13;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=SAB1806c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81495.1; -; Genomic_DNA.
DR   RefSeq; WP_000830380.1; NC_007622.1.
DR   AlphaFoldDB; Q2YU13; -.
DR   SMR; Q2YU13; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   KEGG; sab:SAB1806c; -.
DR   HOGENOM; CLU_006354_1_2_9; -.
DR   OMA; DERFYVH; -.
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: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_1000017364"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01434"
SQ   SEQUENCE   269 AA;  31460 MW;  C0F65B9F5CAB8761 CRC64;
     MKRSDRYSNS NEHFEHMKHE PHYNTYYQPV GKPPKKKKSK RILLKILLTI LIIIALFIGI
     MYFLSTRDNV DELRKIENKS SFVSADNMPE YVKGAFISME DERFYNHHGF DLKGTTRALF
     STISDRDVQG GSTITQQVVK NYFYDNDRSF TRKVKELFVA HRVEKQYNKN EILSFYLNNI
     YFGDNQYTLE GAANHYFGTT VNKNSTTMSH ITVLQSAILA SKVNAPSVYN INNMSENFTQ
     RVSTNLEKMK QQNYINETQY QQAMSQLNR