ID   A0A0X8JWQ2_9FUSO        Unreviewed;       681 AA.
AC   A0A0X8JWQ2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=AXF11_00665 {ECO:0000313|EMBL:AMD95953.1};
OS   Leptotrichia sp. oral taxon 847.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=1785996 {ECO:0000313|EMBL:AMD95953.1, ECO:0000313|Proteomes:UP000065271};
RN   [1] {ECO:0000313|Proteomes:UP000065271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0260 {ECO:0000313|Proteomes:UP000065271};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (FEB-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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; CP014231; AMD95953.1; -; Genomic_DNA.
DR   RefSeq; WP_068158088.1; NZ_CP014231.1.
DR   AlphaFoldDB; A0A0X8JWQ2; -.
DR   STRING; 1785996.AXF11_00665; -.
DR   KEGG; lot:AXF11_00665; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000065271; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..240
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          347..613
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   681 AA;  76466 MW;  8C01A555D5B9E827 CRC64;
     MKKAEKKEKV KKPKKKFRFL PFLFKVFLFF CVIGVGALAY LVYTVNRDTP VDLIDGYAPV
     SPSVIYDMNG NQIDTIMVQN RDPIGIGDIP EDVQNAFLAI EDRKFRSHHG IDFVRTAKAI
     FLTVTGKRRE GGSTITQQLA KNAFLSPEQT VSRKLKEAIL AIEIERKYTK DEILENYLNT
     IYFGQGAYGI KNAAIKYFNR EPKNLTIAQA AILASLPKSP TKYSKLKYAL ERQKIVLHQM
     REYGFITDEQ YNDAINEKIA FKNGDIKSRN EEEQISTSNV APEFTTIVLS ELRKILKISE
     EDQKFLFDGY KVYATVDLDL QRAAYKAFNS NYNLKTRAGL NGALYSIDPS NGFVKAMVGG
     KNYKKGNFNR AISSLRQPGS SFKPIVYLAA LQKKMTMASV MEDSPVKINN WSPKNFDGSY
     RDSMTLDKAI EISNNIIPVK LLQYVGIPKA EKVWRDAGVV GGDFPKNFTL ALGSISTKPS
     DMAMFYAALA NGGYQVEPQY IYKVENKYGE VIYEAKPKMK KVYDSKDVAV LTYMLENAVN
     YGTGQSAKVF KNGQLIPMAG KTGTTSDYVS AWFTGYTPTL ATVVYVGNDD NKSMGTGMTG
     GSAAAPIWKN YMQSVVDLPN YNVGVFEFID DYIKRKDLTT REIDLENGLL DTDGVNKRTM
     LFKAGTEPIE YDNKFRGGIR F
//