MGT_STAAM
ID MGT_STAAM Reviewed; 269 AA.
AC Q99T05;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=SAV1874;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB58036.1; -; Genomic_DNA.
DR RefSeq; WP_000830380.1; NC_002758.2.
DR PDB; 3VMQ; X-ray; 2.52 A; A/B=28-269.
DR PDB; 3VMR; X-ray; 3.69 A; A=28-269.
DR PDB; 3VMS; X-ray; 3.20 A; A/B=28-269.
DR PDB; 3VMT; X-ray; 2.30 A; A/B=28-269.
DR PDB; 5ZZK; X-ray; 2.64 A; A=28-269.
DR PDBsum; 3VMQ; -.
DR PDBsum; 3VMR; -.
DR PDBsum; 3VMS; -.
DR PDBsum; 3VMT; -.
DR PDBsum; 5ZZK; -.
DR AlphaFoldDB; Q99T05; -.
DR SMR; Q99T05; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; Q99T05; -.
DR EnsemblBacteria; BAB58036; BAB58036; SAV1874.
DR KEGG; sav:SAV1874; -.
DR HOGENOM; CLU_006354_1_2_9; -.
DR OMA; DERFYVH; -.
DR PhylomeDB; Q99T05; -.
DR BioCyc; SAUR158878:SAV_RS10260-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002481; 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_0000083154"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01434"
FT HELIX 45..65
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:3VMT"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:3VMT"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:3VMT"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:3VMT"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3VMS"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:3VMT"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3VMQ"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5ZZK"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:3VMT"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:3VMT"
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
