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Database: UniProt
Entry: A0A0G1QA98_9BACT
LinkDB: A0A0G1QA98_9BACT
Original site: A0A0G1QA98_9BACT 
ID   A0A0G1QA98_9BACT        Unreviewed;       785 AA.
AC   A0A0G1QA98;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=UX23_C0012G0015 {ECO:0000313|EMBL:KKU14623.1};
OS   Parcubacteria group bacterium GW2011_GWB1_45_9.
OC   Bacteria.
OX   NCBI_TaxID=1618879 {ECO:0000313|EMBL:KKU14623.1, ECO:0000313|Proteomes:UP000034512};
RN   [1] {ECO:0000313|EMBL:KKU14623.1, ECO:0000313|Proteomes:UP000034512}
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:KKU14623.1}.
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DR   EMBL; LCLK01000012; KKU14623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1QA98; -.
DR   PATRIC; fig|1618879.3.peg.560; -.
DR   Proteomes; UP000034512; 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   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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          56..228
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          320..569
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   785 AA;  87979 MW;  3E351A570F4327B8 CRC64;
     MRRFLVFFFT ISLLGLAGAG AALLFTVRDL PDPSQLGEKQ FVQSTKIYDR TEEILLYEIH
     GDEKRTVVPH EEIPEYVRLA TLAIEDQSFY NHPAFDWKGI ARGIWAGISR GRFQGGSTIT
     QQLARNSFLT PERTIKRKVR ELILALELER QYSKDEILYL YLNQIPYGGN AYGVEAASQL
     YFGKSVRDVN LEEAAILASL VKAPTYYSPW GSHTDELNQR QEYVLAQMFK LDFIDEEEFE
     RAKNAEIKFM PQTIGKIRAP HFVVSVQNYL VQKYGEETIE KGGLKVITTL DWKLQELAEK
     VVAEGAARNE ELYGGRNAAL LAQDAETGQI LAMVGSRDYF DIQNDGNFNV ATQGLRQPGS
     AFKPFVYYAA LQKGYTPDTV IFDVPTEFDT TGNPARSYRP ENFDEKFRGP VTFRQALSQS
     LNLPAVKVLY LAGLDNALNV AKDFGISTLT ERGRYGLSLV LGGGEVKLSE LVNAYSVLAR
     DGIKHEQTTV LKVEESDGRI LEEYKNNEIQ VADPQIIKQI NDILSDENAR RPLFQNSFSQ
     TIVSGHQIAL KTGTTNDYHD AWTIGYTPSL VIGVWAGNNN NQPMHSRGGS ILAAVPIWHT
     FISKALKEKE LKTFARPEPV SSQKPVLNGN FAPSGVVHSI LYYVQKNDPT GPPPSNPATD
     PQFNNWESAV LAWVQMNAPN ILAFSQQNPP QRQSNLDIEF LTPRNGDWIN ENVFVSVNIQ
     SSSPVTKIEL RLNGRLMDSK IGSFSSNIRY DMRLSASVLL TQNELSITAT NAEEVTKEKN
     IILYN
//
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