ID D1PAH4_9BACT Unreviewed; 244 AA.
AC D1PAH4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 ECO:0000313|EMBL:EFB36310.1};
GN ORFNames=PREVCOP_04199 {ECO:0000313|EMBL:EFB36310.1};
OS Segatella copri DSM 18205.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=537011 {ECO:0000313|EMBL:EFB36310.1, ECO:0000313|Proteomes:UP000004477};
RN [1] {ECO:0000313|EMBL:EFB36310.1, ECO:0000313|Proteomes:UP000004477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18205 {ECO:0000313|EMBL:EFB36310.1,
RC ECO:0000313|Proteomes:UP000004477};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) 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 membrane {ECO:0000256|HAMAP-Rule:MF_00766};
CC Single-pass membrane protein {ECO:0000256|HAMAP-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:EFB36310.1}.
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DR EMBL; ACBX02000007; EFB36310.1; -; Genomic_DNA.
DR RefSeq; WP_006846918.1; NZ_VZAC01000004.1.
DR AlphaFoldDB; D1PAH4; -.
DR STRING; 537011.PREVCOP_04199; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; 537011-PREVCOP_04199; -.
DR GeneID; 69849716; -.
DR HOGENOM; CLU_006354_1_1_10; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000004477; 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 membrane {ECO:0000256|HAMAP-Rule:MF_00766};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00766};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00766};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00766,
KW ECO:0000313|EMBL:EFB36310.1}; Membrane {ECO:0000256|HAMAP-Rule:MF_00766};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00766};
KW Reference proteome {ECO:0000313|Proteomes:UP000004477};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00766, ECO:0000313|EMBL:EFB36310.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00766};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00766}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00766"
SQ SEQUENCE 244 AA; 27993 MW; A7F13CA4D643F9DE CRC64;
MILKKIKNIV KWVVVLFFST TILAVVAYRF IPVYVTPLMF IRCFQQVADG ESITLHHHWI
SMDKISPHMP VAVMASEDAR FLKHHGFDFN AIESAAKNNA RGGKVHGAST ISQQTAKNVF
LWPGRSWTRK GFEVYFTFLI EMMWSKQRIM EVYLNSIEMG PGIYGVDAVA EYHFDKKAKD
LFRGECALIA ATLPNPRKFS SLHPSAYMKK RQRQIEHQMR FIPTFPREGE DFDPGTAVGG
YRVK
//
