ID A0A087A020_9BIFI Unreviewed; 818 AA.
AC A0A087A020;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BBIA_1782 {ECO:0000313|EMBL:KFI52120.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI52120.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI52120.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI52120.1,
RC ECO:0000313|Proteomes:UP000029108};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-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:KFI52120.1}.
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DR EMBL; JGYN01000007; KFI52120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087A020; -.
DR STRING; 1437608.GCA_000771645_01660; -.
DR eggNOG; COG0744; Bacteria.
DR Proteomes; UP000029108; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 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:KFI52120.1};
KW Glycosyltransferase {ECO:0000313|EMBL:KFI52120.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
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:UP000029108};
KW Transferase {ECO:0000313|EMBL:KFI52120.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..267
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT REGION 733..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 87683 MW; EF716CBEA78B8C3C CRC64;
MPKKKSPTVA RVLSLIMAYV TLCVAGGIAA SVLLMPAVFA ANKATQALVP SLQVEGIDFD
VTSLPQKSIM YASDGTTKMG EFYEDNRIVV PIKNVSKYMR WAVVAREDKR FFDHAGVDVQ
GVMRAFVKTY VLKQDEQGGS SLTQQYVKNV LITKAESDND PIARYHASEG TVARKIREML
IAVQMEQKYS KLEILQGYLN IAQFGRNRLY GVETAARRYF NVSAKDLNIV QSATIAAITK
NPEKFDPSVE ANLPTAQKQR NTVLQLMYEQ GYITKAECTQ AQKTPIQDTL NIQPLTTGCQ
NAGDYAFFCA YVTQRILNSS EFGKTKEARL QLLKEGGLSI VTTLDVDANS LLMKAARDTV
PPTDPSGFEI MMASVKPGTG EVLGFGINRT YTGGDATDQT QTSMNYMVDA EDGGGAGFPV
GSTIKPFNMV AWMEAGRSIN ENLQTTTSYA TSEFACENYN GKMQNYSGTT ELWPVTNALT
NGTVNPESPF LGLVRSHNTT QASMGAIIGL CRVADAYTQA GYHDASSLKT IDQVPATYNP
AMMIGSVNVS PLTMANMYAT LAADGVECTP IAMKKVTRMN GEEISVPKAN CHQAIDKEIV
QTVAYALNQG TIRSDGAGQY AKLDSGRKTF AKTGTNETMY MATGGFIPKQ IATFVLVGDA
QAPIQNPVAN IAINGTYRGY WDGGTIAAPA WKEFMDAYAD KKGLGKDVGN DYGTPVAKYT
TSSGSVTTIQ GRTLGTYSNT SNSNNGTTNS NGTTGNNSSS NSTGGNSTQS NQSGQSNQSG
QSNGQSSTQS NSGTSSQQGT SNQQSSNSQQ SGTTNSGQ
//
