ID A0A2T0N5P0_9ACTN Unreviewed; 749 AA.
AC A0A2T0N5P0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=B0I32_104437 {ECO:0000313|EMBL:PRX67680.1};
OS Nonomuraea fuscirosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1291556 {ECO:0000313|EMBL:PRX67680.1, ECO:0000313|Proteomes:UP000238312};
RN [1] {ECO:0000313|EMBL:PRX67680.1, ECO:0000313|Proteomes:UP000238312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7104 {ECO:0000313|EMBL:PRX67680.1,
RC ECO:0000313|Proteomes:UP000238312};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-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:PRX67680.1}.
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DR EMBL; PVNG01000004; PRX67680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0N5P0; -.
DR Proteomes; UP000238312; Unassembled WGS sequence.
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:PRX67680.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000238312}.
FT DOMAIN 49..223
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 318..569
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 618..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..695
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 78844 MW; 81A7E7B7A7FEC7FE CRC64;
MVAGVTVLVA GVFGMIMVAY ANTPLPDETQ DQAIEQGSII YYRDGKTEIA RLGTKREIVD
ISRIPRHVQD AFIAAENRTF RTDPGISVSG ITRAVWSTVT GQQVQGGSTI TQEMARGYYD
GLSQERTIQR KVKEIFVAIR AGKEMSKDEI LANYLNTIYF GRGADGIQAA AQAFFDRDVE
KLTPAQAAYL AGRIQSPDAF DAAEAKKNFA PTKERFAYVI DGMGVVDPAK YGSLRTTAKF
PKLARPDKKE TLKGINGYMV DIVQRELERR GITRERLRAE GYRVTTTFDK RLMRAAKKTV
ESNLDAIGDK NIRANMAAVD PRNGRVIAFY SGRDYLKSFT NNAFDANKQA ASAFKPYVLA
AWLESGYSLK SFVSGKGPVT LPGTKPIRNS HDVGAAVQID KATAQSVNTA FATMAQEVGL
EEVEKIAEGA GIDKKDLALA IKDHAYGMSI GAGLVTPVEQ AAGYGIFANG GVHHDAHVVI
SVKAYTGKTV LQEAGKPATV ISPDTAADAT YAMQQVVKNG TAAGTALPGG RPIAGKTGTN
NENKEAWFVG YAPQLSAAVG MYKEVPQRNP KTKKILKDAN GYPLPKEVSL GNIQGAGTPT
KIWRDFMTLA MEGKPVEPFP APAFAGEPHN LVNKPEPKPT KEPDEPGGDD FGTDPACPGD
PSCGAGDPGD GTVDDGGDDG GDTGTSDEDP LGDDGDPTLN DNGDSGSTGD SGGTGDSGGT
GDSGDTGDSG GTGDSGGTGT APTSGPQGG
//
