ID MTGA_AERHH Reviewed; 235 AA. AC A0KK53; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 109. 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}; GN OrderedLocusNames=AHA_2130; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / RC KCTC 2358 / NCIMB 9240 / NCTC 8049; RX PubMed=16980456; DOI=10.1128/jb.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."; RL J. Bacteriol. 188:8272-8282(2006). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000462; ABK38359.1; -; Genomic_DNA. DR RefSeq; WP_011705989.1; NC_008570.1. DR RefSeq; YP_856654.1; NC_008570.1. DR AlphaFoldDB; A0KK53; -. DR SMR; A0KK53; -. DR STRING; 380703.AHA_2130; -. DR CAZy; GT51; Glycosyltransferase Family 51. DR EnsemblBacteria; ABK38359; ABK38359; AHA_2130. DR KEGG; aha:AHA_2130; -. DR PATRIC; fig|380703.7.peg.2131; -. DR eggNOG; COG0744; Bacteria. DR HOGENOM; CLU_006354_1_1_6; -. DR OrthoDB; 9766909at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000756; Chromosome. 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; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane; KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..235 FT /note="Biosynthetic peptidoglycan transglycosylase" FT /id="PRO_1000017298" FT TRANSMEM 12..34 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00766" SQ SEQUENCE 235 AA; 26801 MW; F0F77935E173BE47 CRC64; MRPALARRLL SGLGKLLLAA LLSTIVSVAL LRFIDPPMWT WRLERALFPP AKVAEVKHDW VPLEQISREL QLAVIAAEDQ RFAEHNGFDM DAISSALKHN QHSERVRGAS TLSQQTAKNL FMWSDRSFLR KGIEAWFTLL MELGWDKSRI LEMYLNIVEF GPGIYGAEAA ARHYFGKPAA RLTRYEASLL AAALPNPWRY RVKPPSPYVQ QRSAWIRRQM GQLGQITLNK VHQAD //