MTGA_CUPMC
ID MTGA_CUPMC Reviewed; 233 AA.
AC Q1LIV1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
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}; OrderedLocusNames=Rmet_3053;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF09925.1; -; Genomic_DNA.
DR RefSeq; WP_011517555.1; NC_007973.1.
DR AlphaFoldDB; Q1LIV1; -.
DR SMR; Q1LIV1; -.
DR STRING; 266264.Rmet_3053; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; ABF09925; ABF09925; Rmet_3053.
DR KEGG; rme:Rmet_3053; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_1_0_4; -.
DR OMA; PAPKCFD; -.
DR OrthoDB; 1793788at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002429; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..233
FT /note="Biosynthetic peptidoglycan transglycosylase"
FT /id="PRO_0000257684"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ SEQUENCE 233 AA; 26675 MW; AAF4D2813520C896 CRC64;
MRWLAYLAGC LIVGVVAMQV YFFLQIAAWQ VVNPSSTTFM RAERWRLCGF NFWSCPVQRQ
WVRYDEISRN IKRAVIASED ADFVNHPGYE LDAMLDAWER NKQRGRIVRG GSTITQQLAK
NLFLSSEQNY LRKGQELAIT WMLELWLDKQ RIFEIYLNSV EWGEGVFGVE AAAQHYFHTS
ASKLSVGQAA RLAAALPAPK CFDKKQYCAN VHVNFRVKAS IIARRMGAAT LPD
