ID A0A0Q7PIQ2_9GAMM Unreviewed; 261 AA.
AC A0A0Q7PIQ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Biosynthetic peptidoglycan transglycosylase {ECO:0000256|HAMAP-Rule:MF_00766};
DE EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_00766};
DE AltName: Full=Glycan polymerase {ECO:0000256|HAMAP-Rule:MF_00766};
DE AltName: Full=Peptidoglycan glycosyltransferase MtgA {ECO:0000256|HAMAP-Rule:MF_00766};
DE Short=PGT {ECO:0000256|HAMAP-Rule:MF_00766};
GN Name=mtgA {ECO:0000256|HAMAP-Rule:MF_00766};
GN ORFNames=ASD14_09240 {ECO:0000313|EMBL:KQY51011.1};
OS Lysobacter sp. Root494.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736549 {ECO:0000313|EMBL:KQY51011.1, ECO:0000313|Proteomes:UP000051738};
RN [1] {ECO:0000313|EMBL:KQY51011.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY51011.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY51011.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY51011.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptidoglycan polymerase that catalyzes glycan chain
CC elongation from lipid-linked precursors. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00766};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00766}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00766}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00766}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 51 family.
CC {ECO:0000256|HAMAP-Rule:MF_00766}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQY51011.1}.
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DR EMBL; LMFH01000006; KQY51011.1; -; Genomic_DNA.
DR RefSeq; WP_056132450.1; NZ_LMFH01000006.1.
DR AlphaFoldDB; A0A0Q7PIQ2; -.
DR STRING; 1736549.ASD14_09240; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051738; Unassembled WGS sequence.
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; Biosynthetic peptidoglycan transglycosylase-like; 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 NCBIfam; TIGR02070; mono_pep_trsgly; 1.
DR PANTHER; PTHR30400:SF0; BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30400; MONOFUNCTIONAL BIOSYNTHETIC PEPTIDOGLYCAN TRANSGLYCOSYLASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_00766};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00766};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00766};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00766};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00766};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00766};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00766}; Reference proteome {ECO:0000313|Proteomes:UP000051738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00766};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00766};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00766}.
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00766"
FT DOMAIN 72..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
SQ SEQUENCE 261 AA; 29933 MW; B86E5BF39C7C280B CRC64;
MQDAEQNTVA VAVSPGRRRW RSWLWRLPLL FVAITVLQVL LLRFIDPPFT AFMAARQLEA
VGSGDFGFRV AYDWRDLDDI SRNVPLAMIA SEDQNFANHN GFDFQAIEKA RAHNERAEER
ARKRNKPVKR IRGASTISQQ TAKNLFLWKG QGVTRWARKG LEVWYTLLIE TLWPKSRIIE
VYVNTVELGN GVYGAQAAAR TYFRKDANRL APAEAARMAA VLPNPRRYSI ARPGPYVQRR
SNAIQRQMRY MGGPAFLQRL D
//
