ID A0A136N440_9BACT Unreviewed; 744 AA.
AC A0A136N440;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=UZ09_BCD002000102 {ECO:0000313|EMBL:KXK40939.1};
OS Bacteroidetes bacterium OLB9.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK40939.1, ECO:0000313|Proteomes:UP000070267};
RN [1] {ECO:0000313|EMBL:KXK40939.1, ECO:0000313|Proteomes:UP000070267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB9 {ECO:0000313|EMBL:KXK40939.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023988};
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:KXK40939.1}.
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; LNBW01000003; KXK40939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136N440; -.
DR STRING; 1617420.UZ09_BCD002000102; -.
DR PATRIC; fig|1617420.3.peg.110; -.
DR Proteomes; UP000070267; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 28..195
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 655..741
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 744 AA; 84880 MW; 8ABCA7B2552B5777 CRC64;
MPIPDYKPAF SKQLYARDNR LLSANVSSEQ QWCFPLDEAL PEALKASIIL YEDEYFYWHP
GVNPISAVKA AIQNYKAGRI VRGASTIPMQ IMRIKNRHSQ RTLLNKIWET ISALKYRMFY
NSSHILKEWC EIAPFGGNVI GVKAAALKYF HRPMDKLSWA EYALLAVMPN APTFANLKRN
RAELKRKRDF LLRKLHDKGY FDASELGLYL GEELPTFTGE IPQYGYHLLK YLSKEYSDQS
VYYTTVDYDI QLRTQELLER ESSFLQADDI NNLAAVILDV ESNQLIAYHG NVRSKSGKFS
YVDVAQAPRS YGSLLKPILF AHVLDIGELL PQEMIADIPT VIGDFQPENF DKKFRGAVSF
SDMLIQSLNV PAVRVLNTTG LQSFYDRISR LQVAYLNKGA DHYGLSIILG GGESSLWDLT
RLYKGMARNY AGYSTPFDKV KILKDEVHHK TLSEVTFSAF SIHHTVNTMA DLTRPREEKS
WDLYGTDYKV AWKTGTSYGH RDSWAIGFNG KYAVGVWVGN ETGEGRFGLT GISKAAPVMF
KLFNVLPDNH WFGRPPAYSD HEIIRICSHS GKIAGPLCNQ TKVMDVSKMS YRYVPCTWHK
VVGLDAQGLA LSEDCLSNAV KLDTFFTLPP YMEYYYKQAH INYRIIPAFS PACSRGEQPL
KIIYPNQGVK VFLPKESVSK QQDIVMKAYH RDDKAVLYWF VNDQYIGTTN NGHHEMLFKS
KKGHYQLYIT DQNGHNESVK FDII
//
