ID A0A0X3WDV3_9ACTN Unreviewed; 772 AA.
AC A0A0X3WDV3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ADL30_14785 {ECO:0000313|EMBL:KUL55100.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL55100.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL55100.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL55100.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL55100.1}.
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DR EMBL; LLZK01000188; KUL55100.1; -; Genomic_DNA.
DR RefSeq; WP_062774752.1; NZ_LLZK01000188.1.
DR AlphaFoldDB; A0A0X3WDV3; -.
DR Proteomes; UP000053420; 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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053420}.
FT DOMAIN 77..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 362..630
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 673..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 81222 MW; 3FB5708725247BCC CRC64;
MAKKRSGGGL SPTQQAAKFL GVSVLAGAVL AGIALPAAGA LGLAAKGSVE GFDEIPANLK
QPPLSQRTSI LDNKGGTIAT VYSRDRTVVP LKDISPYMQK AIVAIEDARF YEHGAVDLKG
ILRALNQNAQ SGGVAQGAST LTQQYVKNVF VEEAGDDPTK VAQATQQTLG RKIRELKYAI
QVEEELGKKR ILKNYLNITY FGQQAYGIEA ASQRYFSKPA KDLKLQEAAL LAGIVQSPSR
YDPVNDATEA TQRRNIVLQR MAETHDISQQ EADEAKKTGL GLKVSRPKNG CITAVSGAGF
FCDYVREVFL NDPVFGKTKE ERAKVWNRGG LKIRTTLDPQ TQESVQASIK DHVNKSDDVA
TATTIVEPGT GKVLGMGQSR PYGFQKDETT INLSVDSDMG GGAGYQPGST FKPIVAAAAL
EGGKSAGQRY SSPYEMPYPA RVSTCGGKNW VNSNNEKLTN ENETEVGPYG MREATAKSVN
TYYVQLIGDI GICPVTRMAD KMGVERADGK DMAQAPSIAL GTQETSPLTM ASAYASFASR
GTYCTPIAIE SINTLSGKSL PVPKSTCSRA MSQKTADTIN TLLKGVVEDG TGRQAGLGSR
ASAGKTGTTD FRYAAWFVGY TPNMSGAVWV GDPQHKRQMV DITIGGVPYS KVFGGEVPGP
IWRDAMSGAL AGKPAPGFNT VHIPGGDKDR NRDRDRDGDG GRDQDQDDDK PGAGGGDGDG
GNGDNGGLGD DWPDVEIPPD AIGGLGDGGG NGNGNGGGNG NGGDGGIGGW RP
//
