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Database: UniProt
Entry: A0A1V4D0U0_9ACTN
LinkDB: A0A1V4D0U0_9ACTN
Original site: A0A1V4D0U0_9ACTN 
ID   A0A1V4D0U0_9ACTN        Unreviewed;       660 AA.
AC   A0A1V4D0U0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=VT50_0223410 {ECO:0000313|EMBL:OPF76572.1};
OS   Streptomyces antioxidans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF76572.1, ECO:0000313|Proteomes:UP000033615};
RN   [1] {ECO:0000313|EMBL:OPF76572.1, ECO:0000313|Proteomes:UP000033615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC164 {ECO:0000313|Proteomes:UP000033615};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Streptomyces antioxidans MUSC 164.";
RL   Submitted (DEC-2016) 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:OPF76572.1}.
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DR   EMBL; LAKD02000058; OPF76572.1; -; Genomic_DNA.
DR   RefSeq; WP_046089245.1; NZ_LAKD02000058.1.
DR   AlphaFoldDB; A0A1V4D0U0; -.
DR   OrthoDB; 8865355at2; -.
DR   Proteomes; UP000033615; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          79..253
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          432..610
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   660 AA;  71618 MW;  0DFB86C7CD1A442D CRC64;
     MRLRRWAVAR IQLDYPRAGR RGVTRWLPSW RQIALLFLFC LSSLTGLLSF LYLQTDIPKN
     LNDFATQQDN VYYWADGSEM ARTGPVNRQE VPLHKVPEDV QWAVLAAENA SFYTDSGVSP
     SGLMRAVTRM VTGGETQGGS TITQQYVKNA YLNQRQTFSR KLTEMFMAIK LDDRMSKREI
     LQRYLNTSWF GRGSYGIQRA AYAYYGKDVS ELNASEGALL ASLLKGAGTF DPTLGATNHK
     RAVDRWKWVL DRMVDIGKLS KAERARYTTF PEPKAQPKPE GLTGQVGYLV ETAKAYVSSH
     TDISDADFAL GGYQIHTTFE KPKVQALAKA VKKTRDGNLD PEQRPEDRHV RIGAASVAPG
     GAIRALYGGP GYLEQGFNDA NASNVPAGTS FTPFVYAAAL RDGVLLERNG SRTPVTPSTL
     YDGDNKIAVH TPEGPYWDRG GKIVRATNDG DASYGKVPLR QAIVRSINTP MIQLGMDVGL
     DRVRRASIDA GLLPSSFGAR VPAFSLGTAT PSSIRMASAY GTFAAEGTHY APYSVSGLTH
     GGQRVELHKD RAKRAFSAAV AAQVDDALRG AIQSPDGSAR EAAVAGGEVA GKGGTAQDGT
     SAWFVGYTKK LSTAVSLSRV DPKSQELMPL KGMGGGGADT SGDTYPKDIW KRYMTAGTTE
//
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