ID   MGT_STAS1               Reviewed;         270 AA.
AC   Q49YR9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
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=SSP0919;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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}.
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; AP008934; BAE18064.1; -; Genomic_DNA.
DR   RefSeq; WP_011302787.1; NZ_MTGA01000031.1.
DR   AlphaFoldDB; Q49YR9; -.
DR   SMR; Q49YR9; -.
DR   STRING; 342451.SSP0919; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   PRIDE; Q49YR9; -.
DR   EnsemblBacteria; BAE18064; BAE18064; SSP0919.
DR   KEGG; ssp:SSP0919; -.
DR   PATRIC; fig|342451.11.peg.918; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_1_2_9; -.
DR   OMA; DERFYVH; -.
DR   OrthoDB; 1793788at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006371; 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; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..270
FT                   /note="Monofunctional glycosyltransferase"
FT                   /id="PRO_0000083162"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01434"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  31057 MW;  BCAD57BBE365B01B CRC64;
     MKRSDRYKTY NKPNDSNDSN QLHHNTYFKP VNKPQKKKKG KGIILKLLIP ILIIIGIIIG
     VMYALSLRAD TDELKNITEK ESFVYASDMR DYTKGAFIAM EDERFYKHHG FDVKGTSRAL
     FSTLSDKSVQ GGSTITQQVV KNYYYDNEQS ITRKIKELFV AHRVEKEYDK NEILSFYMNN
     IYYGSDQYTI ESAANHYFGV TTDKNNPNLP QISVLQSAIL ASKINAPSVY NINDMSDNFT
     NRVKTDLEKM KQQGYISNSQ YENAIQELGV