ID A0A0G0L098_9BACT Unreviewed; 818 AA.
AC A0A0G0L098;
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=UT08_C0018G0038 {ECO:0000313|EMBL:KKQ84432.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_38_8.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618570 {ECO:0000313|EMBL:KKQ84432.1, ECO:0000313|Proteomes:UP000034081};
RN [1] {ECO:0000313|EMBL:KKQ84432.1, ECO:0000313|Proteomes:UP000034081}
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:KKQ84432.1}.
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DR EMBL; LBVL01000018; KKQ84432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0L098; -.
DR STRING; 1618570.UT08_C0018G0038; -.
DR PATRIC; fig|1618570.3.peg.1274; -.
DR Proteomes; UP000034081; 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 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 78..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..292
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 379..666
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 89485 MW; 884C32DFD6028BCD CRC64;
MSRGIIENMT KRKKGITSTK SVKRIKSKKV HPRPGKTTKP NLARYKSIID LQESVKKSAK
RHAKFGTLFR KVKLWKKIIF FGTLSAIFLW LFWGIPLPTK LGSQQVPVST KLFDRNGNLL
YEIYADKRSN PVALDELPDY VWQSTISIED KDFYRHYGVS FTGVARAIYK TVVERKLQGG
STLTQQLIKN SLLTSERTIK RKIREFALTL VTETLYSKDQ ILEMYLNQIP YGSTAYGIGA
TSELYFGKQV KDLTLAEAAL LAGLPAAPSR FSPFGAHPEQ AKGRQELVLK RMVEDKYISQ
EDADKAMSEE LKFAKGQELK APHFALWVKE ILAEKYGEAV VEKGGLRVTT TLDLDLQDFA
QNAVASEVAK LKKLDVGNGA AVVTRPATGE ILAMVGSKDY NAVDEDGNVN VILSRRQPGS
SIKPINYALA IKDKKITPST VLADVPTCFS VPGTTAYCPK NYDGDFHGAV QVRFALGNSY
NIPAVRVLAL NGIEHFIDFA KQMGITTFTE SKNYGLSLTL GGGEVRPIDM AEAFGVFANA
GIKQPLIPIL KIADWKGKVL EEVDLDETEL SGDRVLEPDV TFLISHILHD NNARSAAFGS
SSYLNIKGHP EASVKTGTTN DRKDNWTIGY TPLAVVVSWV GNNDNSEMGG AVSGVSGASP
IWNEIMRKVL DKAEDGYYDL IDDSLPSEAS AKEGHVWPMQ PDSVTGANVC ATTGIVPKEG
EASSPEGSGP AGCPTRYEYF LKGTAPSQIA GGFQDVGYDK RTGGFINEET PPEFIETRGQ
NVIYDPLGTF LCLDCPVSPA SQSAKISYPI VAKPTTTP
//
