ID A0A366DNL3_9NOCA Unreviewed; 763 AA.
AC A0A366DNL3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DFR74_104218 {ECO:0000313|EMBL:RBO91515.1};
OS Nocardia puris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=208602 {ECO:0000313|EMBL:RBO91515.1, ECO:0000313|Proteomes:UP000252586};
RN [1] {ECO:0000313|EMBL:RBO91515.1, ECO:0000313|Proteomes:UP000252586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44599 {ECO:0000313|EMBL:RBO91515.1,
RC ECO:0000313|Proteomes:UP000252586};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-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:RBO91515.1}.
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DR EMBL; QNRE01000004; RBO91515.1; -; Genomic_DNA.
DR RefSeq; WP_067503139.1; NZ_QNRE01000004.1.
DR AlphaFoldDB; A0A366DNL3; -.
DR STRING; 1210090.GCA_001613185_00721; -.
DR Proteomes; UP000252586; 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 ECO:0000313|EMBL:RBO91515.1}; 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:UP000252586};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 67..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..288
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 381..644
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..745
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 81813 MW; DCC32F3D7FAB7614 CRC64;
MGSVGKGRGK RDAGRKAAPT HASIAGWKER DTPESRERRA RAEAQARERE APPPRRPRTR
GERVRRLILA LFIMFVAVPA LLFVLVYWSA DIPDPAAVRT NQIATILAAD DTTEIAKVVP
PDGNRTPVPL ADVPKPVRDA VLAAEDRDFY TNPGFSTSGF LRAARDNLLG REDAGGGSTI
TQQYVKNAFL GSERTLTRKM RELIIAAKMS RQWSKDDILA AYLNTIYYGR GTYGIAAASR
AYFAKPPAEL TLAEGAVLAA VIRTPSILDP ETHLPELKAR WQYVLDGMVE MKVLAPGDRD
ATVFPEIVPA TEIPDTDTAR GPEGLIRTQV LRELRESGIS ERDLNTGALR ITTTIDPRAQ
QAALAAVRDR LGPQPPDLRA AVVSIDPRSG AVRAYYGGED GVGYDFAQAP LQTGSAFKVF
AVIAAQQQSI PLSRVLDSSP VTDRGTTITN VDGESCGRCS MAEALKRSLN TSFYRLTMSM
FDGPQAIADA AHQAGIPEEI PGVGKSLTEH GERPLNGIVL GQYLVRPIDM ASAYATIAAS
GMYHQPYFVQ RVVTGDGRVL LDRGNPEHPV GKQMPPGQQR VKPAIAENTL QAMLPIAAYS
NGKALAGGRP SGAKTGTTQL GETRRNKDAW MIGFTPSLST AVWIGTEQSQ PIRTAGGADI
YGSGLPADIW KQMMDDALDG TPVEQFPVEP ASAPANPQPQ GGNPYDILNP PRAPEPQAPQ
TPAPESPQQP EPEPPQGPAI IIPPAPTQQL PADIFPGLGG PAP
//
