ID A0A430FVQ6_9BIFI Unreviewed; 776 AA.
AC A0A430FVQ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=D2E24_0440 {ECO:0000313|EMBL:RSX58080.1};
OS Bifidobacterium samirii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2306974 {ECO:0000313|EMBL:RSX58080.1, ECO:0000313|Proteomes:UP000287470};
RN [1] {ECO:0000313|EMBL:RSX58080.1, ECO:0000313|Proteomes:UP000287470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2033B {ECO:0000313|EMBL:RSX58080.1,
RC ECO:0000313|Proteomes:UP000287470};
RA Lugli G.A., Duranti S., Milani C.;
RT "Characterization of the phylogenetic diversity of five novel species
RT belonging to the genus Bifidobacterium.";
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 -!- 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:RSX58080.1}.
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DR EMBL; QXGK01000003; RSX58080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430FVQ6; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000287470; 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 ECO:0000313|EMBL:RSX58080.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000287470}.
FT DOMAIN 81..270
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 379..697
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 728..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 83174 MW; D1D76911B6AA4102 CRC64;
MGRMPKKNSL TASRVLALLM AYLTLCVAGG VVSSVLLMPA VFGANKVAQA VAPSLKVEGI
DFDVTSLPQK STMYASDGTT KIAEFYEDNR IVVPIKEVST YMQKAIVARE DRRFFDHSGV
DVQGVARAFV NTYLLQKAQQ GGSSLTQQYV KNVLLTQAEQ SGDPIAQYHA SEDTIARKLR
EMLIAVQMEK KYSKYEILQG YLNIAQFGSQ RLYGVETAAR RYFGVSAKDL NIVQSATIAA
ITKNPEHLDP SIEANQEESQ NERNTVLMLM HDQGMITDEE YDEAVNTPLV DTLNIQPMTA
GCANSGEYGF FCSYVTQKIL NSEEFGKTAE ERNSLLKEGG LTIVTTLDVD TSSLLMETAR
NTIPADDPSG FEIMMASVQP GTGEVLGFGI NRTYTGYETD DQTETSMNYM VDAIDGGGSG
YGIGSSIKPF NLVAWMQAGH SINENLQTTT SYPTYEFACD DYSGSSTMYT GGTDSWSVSN
ALTNGTVNPE SPFLGLVRSH NTTMASMGAI IGLCRVADAY TAAGYHDAYS GETIDKSSVY
APAMMIGSIN VSPLTMANMY ATLAADGVEC TPIAMKKVTR MNGEEIDVPK ANCHQAIDSD
IVQTVAYAMN QGTVRSDGAG VYAKLPSGRK TFAKTGTHED LMVSTGGFIP KQIATFVLVG
DAQAPGSNRI ANIAINGVYN SYWDGGTIAA PAWRSFMDAW ADRKGLGTDV GNDYGNPAAK
YTATTGGVTN IKGQTVGGST RSNSGATSNS GTGTTSTDDR NQSAQSDDAD DESDDE
//
