MTGA_NEIMA
ID MTGA_NEIMA Reviewed; 233 AA.
AC P0A0Z3; A1ITV8; O52423; O52424; O52425; O52426; O52427; O52428; O52429;
AC O52430; O52431; O52432; O54548; O54634; O54659;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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}; Synonyms=mtg;
GN OrderedLocusNames=NMA2130;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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; AL157959; CAM09227.1; -; Genomic_DNA.
DR RefSeq; WP_002246789.1; NC_003116.1.
DR AlphaFoldDB; P0A0Z3; -.
DR SMR; P0A0Z3; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; CAM09227; CAM09227; NMA2130.
DR KEGG; nma:NMA2130; -.
DR HOGENOM; CLU_006354_1_0_4; -.
DR OMA; PAPKCFD; -.
DR BioCyc; NMEN122587:NMA_RS10830-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000626; 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..233
FT /note="Biosynthetic peptidoglycan transglycosylase"
FT /id="PRO_0000083131"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00766"
SQ SEQUENCE 233 AA; 26631 MW; 8C85F5BE755E4518 CRC64;
MFRIIKWLIA LPVGIFIFFN AYVYGNIITY RAVAPHRTAF MSMRMKQFEQ EGRDVALDYR
WMPYKRISTN LKKALIASED ARFAGHGGFD WGGIQNAIRR NRNSGKVKAG GSTISQQLAK
NLFLNESRSY IRKGEEAAIT AMMEAVTDKD RIFELYLNSI EWHYGVFGAE AASRYFYQIP
AAKLTKQQAA KLTARVPAPL YYADHPKSKR LRNKTNIVLR RMGSAELPES DTD
