ID A0A0M8Y8W2_9PSEU Unreviewed; 687 AA.
AC A0A0M8Y8W2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=ADK67_26275 {ECO:0000313|EMBL:KOX21639.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX21639.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX21639.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX21639.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-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:KOX21639.1}.
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DR EMBL; LGED01000209; KOX21639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8Y8W2; -.
DR STRING; 1415542.ADK67_26275; -.
DR PATRIC; fig|1415542.3.peg.5643; -.
DR Proteomes; UP000037722; 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}.
FT DOMAIN 51..238
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 355..607
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 483..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 72390 MW; 50C45B01CC43B9F3 CRC64;
MAGVLVAAVL FPVVGGLGLA SNRAADTVDQ TSGELTKAEL PLVTTVLDMH GQPIAYLYDQ
YRVPVPSEGI ADTMKAAIIA IEDKRFFEHK GVDWQGIARA AAKAGVEGET TQGASTLTQQ
YVKNYLAFVV GKGSEEAYEK ATEVTLGRKI SEARIATQLE QKMSKDEILT AYLNVVPFGN
GAYGVGAAAR TYFDTTPDKL TVPQAAMLAG LVNEPSRLNP GSDVDAAIKR RNTVIDRMRD
NGAFGPDARV AEEKAAEYKA TDIGVVPDLK LLPNGCVGAG DGPVYGFFCR YLIDYLEKAG
LPTDELLRGG YTITTTMDPV ATRAAKDAAM AQVPKTQPGI ANAMAVVEPG TDKHRVRALA
ANRDFGNNAD AGQSAYSIPA EVTKFGAGSI YKVFTAASAL ERGVARIDQQ IDVPKTYTSK
VYKDGNKPYT VKNAGDYKDK MTLTEALAQS PNTAFIILEE KAGLNNVVDM AYRLGLRESM
QGVNNEGNPL KADGSNGPSQ GDVYKRDNSG SFTLGAGPTS VLELSNVAAT IVSGGKWCPP
TPVEKVVDRN GRPVPLKEAP CDQAVAPEVA NALAVGMSAD IKPGGTAAGA ASGWNRPMIG
KTGTTENHWS VAFIGATPQF AGAVMTFTDG VAPQVICHGT PPRLCGNNGS GGVYGGQVAA
PTWFNAMRVI HEGKPPAPLP PVDPRYR
//
