ID   MTGA_XANCB              Reviewed;         246 AA.
AC   B0RQA5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766};
DE            EC=2.4.1.129 {ECO:0000255|HAMAP-Rule:MF_00766};
DE   AltName: Full=Glycan polymerase {ECO:0000255|HAMAP-Rule:MF_00766};
DE   AltName: Full=Peptidoglycan glycosyltransferase MtgA {ECO:0000255|HAMAP-Rule:MF_00766};
DE            Short=PGT {ECO:0000255|HAMAP-Rule:MF_00766};
GN   Name=mtgA {ECO:0000255|HAMAP-Rule:MF_00766};
GN   OrderedLocusNames=xcc-b100_1290;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
CC   -!- FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain
CC       elongation from lipid-linked precursors. {ECO:0000255|HAMAP-
CC       Rule:MF_00766}.
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_00766};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00766}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00766}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00766}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00766}.
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DR   EMBL; AM920689; CAP50640.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RQA5; -.
DR   SMR; B0RQA5; -.
DR   KEGG; xca:xcc-b100_1290; -.
DR   HOGENOM; CLU_006354_1_1_6; -.
DR   OMA; PAPKCFD; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001188; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
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_00766; PGT_MtgA; 1.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR011812; Pep_trsgly.
DR   PANTHER; PTHR30400; PTHR30400; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   TIGRFAMs; TIGR02070; mono_pep_trsgly; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW   Peptidoglycan synthesis; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..246
FT                   /note="Biosynthetic peptidoglycan transglycosylase"
FT                   /id="PRO_1000133612"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ   SEQUENCE   246 AA;  27658 MW;  AF10837509D78678 CRC64;
     MGTDGLDDKQ ARPPRRARRS LRWVLAAPLL FAAASVLQVL ALRIIDPPIS TVMVGRYLEA
     WGEGEAGFSL HHQWRDLDEI APSLPISVVA AEDQQFPSHH GFDLQAIEKA RDYNARGGRV
     RGASTISQQV AKNVFLWQGR SWVRKGLEAW YTLLIELFWP KQRILEMYVN VAEFGDGIYG
     AQAAARQFWG KDASRLTPTE SARLAAVLPS PRRYDARRPG AYVQRRTAWI QRQARQLGGP
     GYLQAP