ID A0A1E5KSY7_9ENTE Unreviewed; 784 AA.
AC A0A1E5KSY7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BCR26_05545 {ECO:0000313|EMBL:OEH80980.1};
OS Enterococcus rivorum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=762845 {ECO:0000313|EMBL:OEH80980.1, ECO:0000313|Proteomes:UP000095256};
RN [1] {ECO:0000313|EMBL:OEH80980.1, ECO:0000313|Proteomes:UP000095256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25899 {ECO:0000313|EMBL:OEH80980.1,
RC ECO:0000313|Proteomes:UP000095256};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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:OEH80980.1}.
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DR EMBL; MIEK01000067; OEH80980.1; -; Genomic_DNA.
DR RefSeq; WP_069699967.1; NZ_MIEK01000067.1.
DR AlphaFoldDB; A0A1E5KSY7; -.
DR STRING; 762845.BCR26_05545; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000095256; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; 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 Reference proteome {ECO:0000313|Proteomes:UP000095256};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..264
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 360..623
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 85996 MW; EBAC6FBF0C70E2AA CRC64;
MSTEELGSRS ERHAQKGSIP PSTPTGEQKP KKKRRIVLKT FLVLLLLGCI AFLAGVGLFW
SYARKAQKLD DAKLTATVSS KIHDANNEVI EDLGAEKREI IQANDVPQLL KNAIVSVEDK
RFYKHIGVDP VRILGSAFSN IKGSGGLQGG STLTQQLIKL SYFSTKESDQ TLQRKAQEAW
LAVQLEREKS KDEIITYYIN KVYMANGLYG METAALGYFG KPLAELNLPQ TALLAGMPQA
PNDYDPYAKP EQAKNRRDIV LSTMLENKKI SKSEYEQAIA TPIDDGLQPL QHSSTNRKVI
DNYIKEVIAE VEEKTGKNVN TDGLDIYTNL DMAAQQKLYD IINTGDYVQY PDEDLQVAST
IIDVKTGQVK AQIGGRKVPD DVQLGTNQAV ETNRDVGSTV KPITDYGPAI ENLNYSTGKI
MYDKPTTYPG TNINVKNVDL QYMGAITMRT ALIHSRNTTA IQTFEAVGKD NSAAFLKNLG
IEYKTLEYAN AISSNTSEKD RSKYGISSLK LAGAYATFAN EGVYNEPYYV SKVVYQDGSV
DEIKPESRRA IKDSTAYMMT DMLKDVIGTG TAINAQIPGL IQAGKTGTSN YTEEDMAKIG
PVSTMVAPDS TFVGYTPNYA ISVWTGYKDF LRPLPYENWS ISTDVYREMM TYLSQNISAN
DWVMPDSVVQ IGSELYVRGA TQQEGPVFED TTNGSSSVTK ESTLQSQSAP PTSKVESVPT
PPLPPSQESI DSTPESVPTP ESVPTPESVP TPESVPSSEG TINSIPPAQQ SNRNARSENK
KRAS
//
