ID A0A1L8SUC4_9ENTE Unreviewed; 792 AA.
AC A0A1L8SUC4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=RV00_GL002454 {ECO:0000313|EMBL:OJG35700.1};
OS Enterococcus devriesei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=319970 {ECO:0000313|EMBL:OJG35700.1, ECO:0000313|Proteomes:UP000183700};
RN [1] {ECO:0000313|EMBL:OJG35700.1, ECO:0000313|Proteomes:UP000183700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22802 {ECO:0000313|EMBL:OJG35700.1,
RC ECO:0000313|Proteomes:UP000183700};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG35700.1}.
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DR EMBL; JXKM01000005; OJG35700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8SUC4; -.
DR STRING; 319970.RV00_GL002454; -.
DR Proteomes; UP000183700; Unassembled WGS sequence.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12800; -; 1.
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:SF32; PENICILLIN-BINDING PROTEIN 2A; 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 98..283
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 409..652
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 86887 MW; C113934A4424C52F CRC64;
MNFLAHKKKM NRQSKKSSKG KSRTSMGGPF ALNVSLRVVK SLLLGFVVVL FLGGMLALGV
GAGYFAHLVE GTPTPTKSEM KQKVGDIAES SKLLYADNQE LATIQADPIR EKINADEISP
WVKKALVATE DENFYEHPGV VPKAVVRALL GEVIGFGAGS GGSTLTQQLI KQQVLTNETS
FKRKANEIVL ALDVEKYLSK DEILTAYLNV SPFGRNNKGQ NIAGVEEAAI GIFGVHAKDL
NLPQSAFIAG LPQSPIVYSP YTNTGDLKQD YSLGMDRKND VLFNMYREQV ISKKEYDDAK
NYDLAKDFQA RQDVEVQQHG FLYYTIYNEA ISIVAKQQAK EDGISDADYA KTEVSTRYIE
QAKVKMQNQG LIVHSTIDKN IYDAMQLGVA QYGQNLDDGS GTTVETGSVL MDNKTGRIYG
FVGSRDYSSN QNNHAFDTAR QAGSSIKPVL VYGPAIDQGL LGSESRIADF PMKYQHGEDA
GKALENAENK GSKTFQTTRD AIAQSTNIPA YHVYQDMLAK KGSDQFAYDN YLKKMNYPAS
HDWGVEAAPL GTTNVSTLTE VNGFQTLAND GVYQQGYLID SITDSTGKEV YKHANAPVQV
FSKATASIMN DLMRSVIDEQ RTTPFKPILS GINYPLSTAD WVGKTGTTDN YSDNWLIVST
PSITLGSWTG RDDNKPMADG AGNRTATYMA YLADRIYQVN PTIFAESEKF ELSDDVNQVK
VSSFTGLKPG KVSQNGTTYQ VPGGETTSLW AKDGPAENKY DFGIGGNDDE YKTYWNTRNK
TAAKAKEDKT DD
//
