MGT_STAAW
ID MGT_STAAW Reviewed; 269 AA.
AC Q7A0I6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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=MW1814;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB95679.1; -; Genomic_DNA.
DR RefSeq; WP_000830380.1; NC_003923.1.
DR PDB; 3HZS; X-ray; 2.10 A; A=68-268.
DR PDB; 6FTB; X-ray; 2.10 A; A=68-268.
DR PDBsum; 3HZS; -.
DR PDBsum; 6FTB; -.
DR AlphaFoldDB; Q7A0I6; -.
DR SMR; Q7A0I6; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; BAB95679; BAB95679; BAB95679.
DR KEGG; sam:MW1814; -.
DR HOGENOM; CLU_006354_1_2_9; -.
DR OMA; DERFYVH; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q7A0I6; -.
DR Proteomes; UP000000418; 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 1: Evidence at protein level;
KW 3D-structure; 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_0000083158"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01434"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:3HZS"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:3HZS"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:3HZS"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:3HZS"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:3HZS"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3HZS"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:3HZS"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:3HZS"
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
