MTGA_NEIME
ID MTGA_NEIME Reviewed; 165 AA.
AC P69345; O52423; O52424; O52425; O52426; O52427; O52428; O52429; O52430;
AC O52431; O52432; O54548; O54634; O54659;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Biosynthetic peptidoglycan transglycosylase {ECO:0000250|UniProtKB:P46022};
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P46022};
DE AltName: Full=Glycan polymerase {ECO:0000250|UniProtKB:P46022};
DE AltName: Full=Peptidoglycan glycosyltransferase MtgA {ECO:0000250|UniProtKB:P46022};
DE Short=PGT {ECO:0000250|UniProtKB:P46022};
DE Flags: Fragment;
GN Name=mtgA {ECO:0000250|UniProtKB:P46022}; Synonyms=mtg;
OS Neisseria meningitidis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Allele 1 to allele 16;
RX PubMed=9501229; DOI=10.1073/pnas.95.6.3140;
RA Maiden M.C.J., Bygraves J.A., Feil E., Morelli G., Russell J.E., Urwin R.,
RA Zhang Q., Zhou J., Zurth K., Caugant D.A., Feavers I.M., Achtman M.,
RA Spratt B.G.;
RT "Multilocus sequence typing: a portable approach to the identification of
RT clones within populations of pathogenic microorganisms.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3140-3145(1998).
CC -!- FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain
CC elongation from lipid-linked precursors.
CC {ECO:0000250|UniProtKB:P46022}.
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;
CC Evidence={ECO:0000250|UniProtKB:P46022};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000250|UniProtKB:P46022}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P46022}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P46022}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC {ECO:0000250|UniProtKB:P46022}.
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DR EMBL; AF037814; AAC08817.1; -; Genomic_DNA.
DR EMBL; AF037815; AAC08818.1; -; Genomic_DNA.
DR EMBL; AF037816; AAC08819.1; -; Genomic_DNA.
DR EMBL; AF037817; AAC08820.1; -; Genomic_DNA.
DR EMBL; AF037818; AAC08821.1; -; Genomic_DNA.
DR EMBL; AF037819; AAC08822.1; -; Genomic_DNA.
DR EMBL; AF037820; AAC08823.1; -; Genomic_DNA.
DR EMBL; AF037821; AAC08824.1; -; Genomic_DNA.
DR EMBL; AF037822; AAC08825.1; -; Genomic_DNA.
DR EMBL; AF037823; AAC08826.1; -; Genomic_DNA.
DR EMBL; AF037824; AAC08827.1; -; Genomic_DNA.
DR EMBL; AF037825; AAC08828.1; -; Genomic_DNA.
DR EMBL; AF037826; AAC08829.1; -; Genomic_DNA.
DR EMBL; AF037827; AAC08830.1; -; Genomic_DNA.
DR EMBL; AF037828; AAC08831.1; -; Genomic_DNA.
DR EMBL; AF037829; AAC08832.1; -; Genomic_DNA.
DR AlphaFoldDB; P69345; -.
DR SMR; P69345; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR UniPathway; UPA00219; -.
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-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; -; 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..>165
FT /note="Biosynthetic peptidoglycan transglycosylase"
FT /id="PRO_0000083133"
FT VARIANT 6
FT /note="M -> V (in allele 2, allele 4, allele 7, allele 8,
FT allele 12 and allele 15)"
FT VARIANT 9
FT /note="K -> D (in allele 15)"
FT VARIANT 9
FT /note="K -> N (in allele 1, allele 2, allele 4, allele 7,
FT allele 8, allele 9, allele 10, allele 11, allele 12 and
FT allele 16)"
FT VARIANT 13
FT /note="T -> V (in allele 1, allele 2, allele 4, allele 7,
FT allele 8, allele 9, allele 10, allele 11, allele 12 and
FT allele 16)"
FT VARIANT 26
FT /note="R -> H (in allele 4, allele 8, allele 12 and allele
FT 15)"
FT VARIANT 50
FT /note="K -> E (in allele 10 and allele 15)"
FT VARIANT 53
FT /note="A -> T (in allele 15)"
FT VARIANT 75
FT /note="I -> L (in allele 15)"
FT VARIANT 110
FT /note="V -> G (in allele 15)"
FT VARIANT 110
FT /note="V -> I (in allele 7)"
FT VARIANT 122..123
FT /note="QI -> KK (in allele 15)"
FT VARIANT 127
FT /note="K -> D (in allele 15)"
FT VARIANT 129
FT /note="T -> S (in allele 7, allele 8, allele 9, allele 10,
FT allele 11 and allele 14)"
FT VARIANT 139
FT /note="R -> C (in allele 16)"
FT VARIANT 144
FT /note="L -> I (in allele 13)"
FT VARIANT 164
FT /note="R -> K (in allele 5, allele 10, allele 13 and allele
FT 15)"
FT NON_TER 1
FT NON_TER 165
SQ SEQUENCE 165 AA; 18786 MW; 00A7B71CD976BE11 CRC64;
LDYRWMPYKR ISTNLKKALI ASEDARFAGH GGFDWGGIQN AIRRNRNSGK VKAGGSTISQ
QLAKNLFLNE SRSYIRKGEE AAITAMMEAV TDKDRIFELY LNSIEWHYGV FGAEAASRYF
YQIPAAKLTK QQAAKLTARV PAPLYYADHP KSKRLRNKTN IVLRR
