ID A0A387BGP3_9LACT Unreviewed; 820 AA.
AC A0A387BGP3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=D7I46_12475 {ECO:0000313|EMBL:AYG01798.1};
OS Lactococcus allomyrinae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2419773 {ECO:0000313|EMBL:AYG01798.1, ECO:0000313|Proteomes:UP000269374};
RN [1] {ECO:0000313|EMBL:AYG01798.1, ECO:0000313|Proteomes:UP000269374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1JSPR-7 {ECO:0000313|EMBL:AYG01798.1,
RC ECO:0000313|Proteomes:UP000269374};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 1JSPR-7.";
RL Submitted (SEP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP032627; AYG01798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387BGP3; -.
DR KEGG; lact:D7I46_12475; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000269374; Chromosome.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000269374};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..287
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 428..664
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 88382 MW; C035FD0BE2A1E213 CRC64;
MKKDPIDSKE EIENRLQDKM EARRRQKKAN SAKITKKQAK SDDTGDSKTA WSTTFSVVRG
VSVIFGIIFV MLGVFGTAAG IGYFARLVET TKVPAKSEML AKINDIHGVS VINYSNGQPI
SDISSDLVRV TVAGDAISNN VKNALISTED DTFKTNDGVV PKAVVRGILG SVGGGTSSGG
STLTQQLIKQ QILGDSVTFQ RKASEIVYAR ALNNYLTKDQ ILTDYLNVSP FGRNNKGQNI
AGVQEAALGI FGKSAKDLSV PEAAFIAGLP QSPIVYSPYN ADGSLKSKEM LSYGLSRQKD
VLFNMYRGGY ITKADYDKYK VYDISKEFLQ PAAAQSQEHG YLYNVAYTEA VNHIYDYLVQ
RDKVSATELG NDSTKQHYRD LAEQALQNDG YEVTTTINQT IYSAMQTAVA QHGGELQDGT
GEVQTGNVLM DNSTGAVIGF VGGLNYAQNQ NNHAFDTQRS PGSSIKPVLA YGPAIDMGLM
GSATMLSNYP AKYSSGQDIM HVGEKGSNTM MPLGEALDVS WNIPAYWTYQ DILKSGRSSE
PYMSKMGYDI KDYSVESLPL GGGVDPTVVQ HTNGYQTLAN GGVYEPYYVV QSIKDDTGKV
IYQHQNKPTQ VYSEATSTIM EYLLNNVITS QKTSTFYGVL SQINPSLAQN VQWTGKTGTT
DDYTDGWLML STPTVTLGSW IGHDNNSPMG SLTPYSKNGT YMANLVNAIN AADPTIFGPG
KKFPDPNKDP NVTKSKVLVS TGEKAGKISG GALNGVSISG ATTTSFWATK AGAPVTQYNF
AIGGSSSDVA DAWSKILPNY KSEITKSSTT PSSSSKKANN
//
