ID MTGA_SHEAM Reviewed; 245 AA. AC A1S3J2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 95. 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=Sama_0740; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=326297; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1098 / SB2B; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., RA Richardson P.; RT "Complete sequence of Shewanella amazonensis SB2B."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000507; ABL98948.1; -; Genomic_DNA. DR AlphaFoldDB; A1S3J2; -. DR SMR; A1S3J2; -. DR STRING; 326297.Sama_0740; -. DR CAZy; GT51; Glycosyltransferase Family 51. DR KEGG; saz:Sama_0740; -. DR eggNOG; COG0744; Bacteria. DR HOGENOM; CLU_006354_1_1_6; -. DR OrthoDB; 9766909at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000009175; 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..245 FT /note="Biosynthetic peptidoglycan transglycosylase" FT /id="PRO_1000062229" FT TRANSMEM 29..49 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00766" SQ SEQUENCE 245 AA; 27654 MW; 490FD046D145FE61 CRC64; MSEKDLGGGK KAGFIARTWR GFWRWSARLL VAFLILSLVL VATVSVINPP TWAWRIDRAL FPPKEDIQVR HQWVPLDKIA AHMQLAVIAA EDQRFTLHNG VDFAAIKTAI ADRDPGEPLR GASTLTQQTA KNLFLWSSRS FVRKGLEAWF ALLLDTLSGK RRTLELYLNI VEFGPGIYGV EAASRYYFNK GAGKLSTREA ALLAALLPNP WSYRINPPTA YMNRRADWIA RQMRQLGMAT LKDLD //