MGT_STAAC
ID MGT_STAAC Reviewed; 269 AA.
AC Q5HEQ0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=SACOL1932;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38373.1; -; Genomic_DNA.
DR RefSeq; WP_000830380.1; NC_002951.2.
DR AlphaFoldDB; Q5HEQ0; -.
DR SMR; Q5HEQ0; -.
DR IntAct; Q5HEQ0; 4.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAW38373; AAW38373; SACOL1932.
DR KEGG; sac:SACOL1932; -.
DR HOGENOM; CLU_006354_1_2_9; -.
DR OMA; DERFYVH; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000530; 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_0000083153"
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