ID   MGT_STAA2               Reviewed;         269 AA.
AC   A6U2X8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=SaurJH1_1962;
OS   Staphylococcus aureus (strain JH1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=359787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT   JH1.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000736; ABR52796.1; -; Genomic_DNA.
DR   RefSeq; WP_000830384.1; NC_009632.1.
DR   AlphaFoldDB; A6U2X8; -.
DR   SMR; A6U2X8; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   KEGG; sah:SaurJH1_1962; -.
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_1000087439"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01434"
SQ   SEQUENCE   269 AA;  31428 MW;  D4A9109F47A0976A CRC64;
     MKRSDRYSNS NEHFEHMKHE PHYNTYYQPV GKPPKKKKSK RILLKILLTI LIIIALFIGI
     MYFLSTRDNV DELRKIENKS SFVSADNVPE YVKGAFISME DERFYNHHGF DLKGTTRALF
     STISDRDVQG GSTITQQVVK NYFYDNDRSF TRKVKELFVA HRVEKQYNKN EILSFYLNNI
     YFGDNQYTLE GAANHYFGTT VNKNSTTMSH ITVLQSAILA SKVNAPSVYN INNMSENFTQ
     RVSTNLEKMK QQNYINETQY QQAMSQLNR