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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//