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Database: UniProt
Entry: A0A0G1DJP2_9BACT
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Original site: A0A0G1DJP2_9BACT 
ID   A0A0G1DJP2_9BACT        Unreviewed;       700 AA.
AC   A0A0G1DJP2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=UV41_C0006G0028 {ECO:0000313|EMBL:KKS71076.1};
OS   Candidatus Daviesbacteria bacterium GW2011_GWA2_42_7.
OC   Bacteria; Candidatus Daviesbacteria.
OX   NCBI_TaxID=1618425 {ECO:0000313|EMBL:KKS71076.1, ECO:0000313|Proteomes:UP000034785};
RN   [1] {ECO:0000313|EMBL:KKS71076.1, ECO:0000313|Proteomes:UP000034785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKS71076.1}.
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DR   EMBL; LCEJ01000006; KKS71076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1DJP2; -.
DR   PATRIC; fig|1618425.3.peg.147; -.
DR   Proteomes; UP000034785; 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: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: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   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        32..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..256
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          347..621
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          652..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  76837 MW;  B9936818904B5EDB CRC64;
     MAFKRIKNHT VYSGHSTGFR HSLRRAKFLS RFSTLMLTMI LGGIAVLILV IVVFATQVPS
     PRELTSREMA QATKIYDRNG ELLYDIFKDQ NRTPVKLSEV PLVVKQATIA IEDKDFYKHQ
     GFSPLGITRS VFDLIISRKV EGGGSTLTQQ LVKNALLSGE RTLTRKLKEF ILAIQVERAY
     GKDQILEMYL NEIPYGGTAY GIEAAANLYF GKHAKDLDLA ESSLLAGLPQ RPSVYSPYGT
     HPELSKERQV EVLRRMTEDG YITKQQAEEA KNKELTYRTK QNEVGFKAPH FVLYVKQKLI
     EQFGDKLVEQ GGLKVTTTLD YKLHEESQKV VKDEVSKLKN YKVGNAAAVV LDPKNGQILA
     MVGSKDYFAD SEPENCSEGE SCVFEANVNA TLSLRQPGSA TKPITYSAAL QKGYTASTVL
     VDVKTEFPGG DQPAYIPVNY DGQFRGPVQV RYALGNSYNI PAVKTLALTG VKNVMELGYR
     MGLSTWEPTT ENINNAGLSL TLGGREVRLL DLTSAFGVLA NSGVKQDPVS ILKVSDAKDK
     TLYEYRQSDG TRIFEEGIAF IISNILSDNG ARSAAFGTNS VLNISGKTVS VKTGTTDEKK
     DNWTIGYTPS VVVGVWVGNN NNAVMNPAIA SGITGASPIW QKIMIAALKG KDDEKPEAPG
     NVSYVEVDGL MGGKPRDGSP TRREYYIKGT EPSSASSVYR
//
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