ID A0A3D9SCM8_9BACL Unreviewed; 711 AA.
AC A0A3D9SCM8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A8990_107176 {ECO:0000313|EMBL:REE89078.1};
OS Paenibacillus taihuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1156355 {ECO:0000313|EMBL:REE89078.1, ECO:0000313|Proteomes:UP000256304};
RN [1] {ECO:0000313|EMBL:REE89078.1, ECO:0000313|Proteomes:UP000256304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10966 {ECO:0000313|EMBL:REE89078.1,
RC ECO:0000313|Proteomes:UP000256304};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2018) 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:REE89078.1}.
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DR EMBL; QTTN01000007; REE89078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9SCM8; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000256304; 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: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 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 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..245
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 342..619
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 634..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 76503 MW; 1F48E8139A1DBEE9 CRC64;
MNSNRSKENK KESTKKRQIG WTKITVSLII AAAFIFIVGW VTLRTLVDRQ DISLLAKPLP
VETVIMDDQE KEASRIALNT TIEPVSYETL PKPLIDAVVA VEDKRFFEHH GTDLWGIGRA
LFTNVTSGKT VEGASTITQQ LAKNVFLSQE RTWSRKWNEA LLAKKIEQTY TKQQIIEMYL
NQIYFGEGAW GIKRAASVYF GKSVEKLTLS ESAMLAGIIR APSALSPVKH MKEAKERRNV
VLGLMRDQGK ISATTYETAS KLPIRLSSTT ASNGSGIKYA YFVDQIIREA SEQYGLSENE
VLHGGLRIYT TLNTKMQQAA EHVYAQASVF PTSSKDQLIQ SGAVLLDPRD GGIKALIGGR
GNQPFRGFNR AVQLKRQPGS TMKPISVYTP AFERGYQPGD TLMDEPVDFG GYAPKNAGGG
YHGEVSIYDA IVHSYNIPAV ELLNEMGIDA GMEAAERFGI KLSDADRTLG LALGGLQEGV
SPLDMADAFS VFANDGKRYA AHAIVRIESA DGELLAEAAP PAAMTVIEPA VARTMTAMLQ
GVVQEGTGEA AAIDGRAIAG KTGTTELPGT GGEGIKDNWF VGYTPQVVGA VWLGYDHTDA
SHYLTTTSKA AAAVFHSLMS EALKDEPVLE FPPALGLMGK KPNGKPDKNE DAPGLKPGKG
PGKGPGKGPG KGPGIGHDQP PGQQKPGKPK DEHKGHGEHG PGKKKGKHGD D
//
