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Database: UniProt
Entry: A0A0G0R185_9BACT
LinkDB: A0A0G0R185_9BACT
Original site: A0A0G0R185_9BACT 
ID   A0A0G0R185_9BACT        Unreviewed;       725 AA.
AC   A0A0G0R185;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=UT44_C0016G0023 {ECO:0000313|EMBL:KKR16305.1};
OS   Candidatus Levybacteria bacterium GW2011_GWA1_39_32.
OC   Bacteria; Candidatus Levybacteria.
OX   NCBI_TaxID=1618454 {ECO:0000313|EMBL:KKR16305.1, ECO:0000313|Proteomes:UP000034624};
RN   [1] {ECO:0000313|EMBL:KKR16305.1, ECO:0000313|Proteomes:UP000034624}
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:KKR16305.1}.
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DR   EMBL; LBWU01000016; KKR16305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0R185; -.
DR   PATRIC; fig|1618454.3.peg.361; -.
DR   Proteomes; UP000034624; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          36..211
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          301..575
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          679..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..725
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  79645 MW;  D633D80D05FC2174 CRC64;
     MLTAFLFIWY SRDLPQPGKL AEAALGNSTR IYDRKGKILY SVDQDEVKNY VKLKDVPKIV
     KEATIATEDK DFYKNQGFSL TGVIRGLLID PILRRRITGG STITQQLIKN VLLTSERTIP
     RKIKELILAV QVDKIYSKDQ ILEMYLNNVP FGGTAIGIDA AAETYFGKSA KDLNLAQSAF
     LAGLPQAPSL YSPFSGNKYY IDRSTYVLGQ MARQGYITNP EAQKALEEIK RFKFTQRNTA
     IKAPHFVMYV REQIAERFGD AAVDVGGLQI KTSLDYDIQK KTEEIVKSEI ARLKGYRVGN
     GSAIVMDPKT GEILAMVGSE DYFNEENDGN FNASLSRRQP GSSLKPVMYA TALEKGYTAA
     TLIMDVKTDF PTQTTGMYTP VNYDGKFRGP TQLRFALGNS LNIPAVKMLA RVGIKDTMEK
     GYDMGIKNWE PTQKNLSNVG LSLVLGGREV SLLEEVSAYS VLANRGVRQE PLSVLEVKDL
     KGKTLFKQKS VKGPKVLSEE AAFIISHILL DNNARSDAFG SSSFLNIPGK TVSVKTGTTD
     SKRDNWTVGY TPSFVVGVWV GNNDNSPMNP IIASGVTGAS PIWNKIMGSV LKGKTDESLI
     KPANVIAAQI DAFGGGATID GQSTRSEYFI KGTEPTSKAP IYKEKDGKRY IVIRESDPVS
     TDGKNRWQEG IDAWIEQNHA GDELWHAPGS VFEEPKKKDE PTPTPSVTPS PTPTPTPTPL
     IPPGP
//
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