MGT_STAA8
ID MGT_STAA8 Reviewed; 269 AA.
AC Q93Q23; Q2G2G8; Q53720;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Monofunctional glycosyltransferase {ECO:0000255|HAMAP-Rule:MF_01434, ECO:0000303|PubMed:11466281};
DE Short=MGT {ECO:0000255|HAMAP-Rule:MF_01434, ECO:0000303|PubMed:11466281};
DE EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_01434, ECO:0000269|PubMed:11466281};
DE AltName: Full=Peptidoglycan TGase {ECO:0000255|HAMAP-Rule:MF_01434, ECO:0000305};
GN Name=mgt {ECO:0000255|HAMAP-Rule:MF_01434, ECO:0000303|PubMed:11466281};
GN OrderedLocusNames=SAOUHSC_02012;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=11466281; DOI=10.1128/jb.183.16.4779-4785.2001;
RA Wang Q.M., Peery R.B., Johnson R.B., Alborn W.E., Yeh W.-K., Skatrud P.L.;
RT "Identification and characterization of a monofunctional
RT glycosyltransferase from Staphylococcus aureus.";
RL J. Bacteriol. 183:4779-4785(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7905453; DOI=10.1016/0378-1119(93)90016-v;
RA Borchardt S.A., Babwah A.V., Jayaswal R.K.;
RT "Sequence analysis of the region downstream from a peptidoglycan hydrolase-
RT encoding gene from Staphylococcus aureus NCTC8325.";
RL Gene 137:253-258(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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 ECO:0000269|PubMed:11466281}.
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, ECO:0000269|PubMed:11466281};
CC -!- ACTIVITY REGULATION: Activity increases 3-fold at pH 6.1. Inhibited by
CC moenomycin A. {ECO:0000269|PubMed:11466281}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01434, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01434,
CC ECO:0000269|PubMed:11466281}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01434}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC {ECO:0000255|HAMAP-Rule:MF_01434, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA18515.1; Type=Erroneous termination; Note=Truncated C-terminus. May be due to a cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF287468; AAK83040.1; -; Genomic_DNA.
DR EMBL; L19300; AAA18515.1; ALT_SEQ; Unassigned_DNA.
DR EMBL; CP000253; ABD31068.1; -; Genomic_DNA.
DR RefSeq; WP_000830380.1; NZ_LS483365.1.
DR RefSeq; YP_500509.1; NC_007795.1.
DR AlphaFoldDB; Q93Q23; -.
DR SMR; Q93Q23; -.
DR STRING; 1280.SAXN108_1904; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; ABD31068; ABD31068; SAOUHSC_02012.
DR GeneID; 3920466; -.
DR KEGG; sao:SAOUHSC_02012; -.
DR PATRIC; fig|93061.5.peg.1827; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_1_2_9; -.
DR OMA; DERFYVH; -.
DR BioCyc; MetaCyc:MON-15458; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:Q93Q23; -.
DR Proteomes; UP000008816; 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:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
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 Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..269
FT /note="Monofunctional glycosyltransferase"
FT /id="PRO_0000083152"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01434"
FT CONFLICT 257..258
FT /note="Missing (in Ref. 1; AAK83040)"
FT /evidence="ECO:0000305"
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
