ID A0A3M2LAG3_9NOCA Unreviewed; 749 AA.
AC A0A3M2LAG3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=EBN03_06030 {ECO:0000313|EMBL:RMI34404.1};
OS Nocardia stercoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=2483361 {ECO:0000313|EMBL:RMI34404.1, ECO:0000313|Proteomes:UP000279275};
RN [1] {ECO:0000313|EMBL:RMI34404.1, ECO:0000313|Proteomes:UP000279275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-LL90 {ECO:0000313|EMBL:RMI34404.1,
RC ECO:0000313|Proteomes:UP000279275};
RA Ling L.;
RT "Isolation from cow dung.";
RL Submitted (OCT-2018) 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:RMI34404.1}.
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DR EMBL; RFFH01000002; RMI34404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2LAG3; -.
DR Proteomes; UP000279275; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF34; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 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:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000279275};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..265
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 356..609
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..703
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 78729 MW; 5DF998EEC3591206 CRC64;
MRQGLQMRPV RHRAPAPAAP ADTDTGTRAA VADWTRSGRR AGRLVLALFL IFLVVPALLC
ALAYWSAQVP RPSAVQTNQI ATVTAADGTT VLAKIIPPEG NRTLVKLDDV PMPVRDAVLA
AEDRNFYSNP GFSTQAFLRA ARDNLLGRQD AGGGSTITQQ YVKNAFLDSE RSLTRKMREL
IISAKMARQW SKDDILAAYL NTIYYGRGAY GISAAARAYF DKHVPDLTLA EGAVLASVIR
TPSLLDPETH HDQLVARWNY VLDGMVTMGK LTPDQRAAQQ FPNIIGPSAL DDATHTPNGL
IRTRVLDEMR AAGITDDEIN TGALRITTTI DRRAQQAAVD AVHSTLDNQP PDLRTAVVSI
DPRTGAVRAY YGGDDGVGYD FAQAPLQTGS SFKTFAVLAA VQQNVPLSYQ LDSGPITVNG
VSVSNVGNET CGTCSLAEAF KRSLNTSFYR LTETVGPQAV ADAAHAAGIP ERIPGVAGTS
LTDSDTGTPS PSIALGVYSV RPIDMASAYA TLAASGMYHS PYFVQKVVTG DGRVLLDHGN
PAGTLRVTAA AADTTTHAML PIAGYSNGHD LAGRPSAAKT GTTQLGDTGA DKDAWMIGFT
PSLSTAVWIG TEQPQAITTR WGGPIYGSGL PADIWKRTMD GALADSPVEQ FAQPTDPPLL
LDPGPPPPGE APAPPAPAPA WSGPDPSAIG PAAPAPAPAP QQAPLRGGPF DTPDPGPPPE
DPAPGLLVPP PNTPREVQIL PGLTIQLPG
//
