ID A0A0G0MAP5_9BACT Unreviewed; 762 AA.
AC A0A0G0MAP5;
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=UT24_C0014G0008 {ECO:0000313|EMBL:KKR00268.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_39_12.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618574 {ECO:0000313|EMBL:KKR00268.1, ECO:0000313|Proteomes:UP000033881};
RN [1] {ECO:0000313|EMBL:KKR00268.1, ECO:0000313|Proteomes:UP000033881}
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:KKR00268.1}.
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DR EMBL; LBWB01000014; KKR00268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MAP5; -.
DR STRING; 1618574.UT24_C0014G0008; -.
DR PATRIC; fig|1618574.4.peg.1115; -.
DR Proteomes; UP000033881; 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 84..259
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 346..614
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 84051 MW; AB6A8E07EF10AE02 CRC64;
MAKTKTKKLK NLKTKESRNK KHQPRSEKKS KIRSLFKNVR LWKKVLFLGI LSAIFSWLFW
GIPLPTKLSK EEVPVSTKLF DRNGKLIYEI YAERKSTPVK LDELPDYIWE STVAIEDKDF
YKHYGVSFTG VMRAVYKTLV KQKLQGGSTL TQQLIKNALL TPERTLKRKI REFALTLVVE
TIYSKDQILE MYLNQIPYGG TSYGIGAASE TYFGKNAKDL TLAEATLLAG LPAAPSYYSP
YGAHPELSKG RQEVVLMQMV EEGYIIQEDA DKAKEEELKY AEPEKLRAPH FALWVKNLLA
EKYGEATTEK GGLRVTTTLD LELQEFAEVA VATEVAKLKK QNVGNGAALV TRPATGEILA
MVGSKDYFAE DEDGKVNIVF AKRQPGSSIK PLNYALAIKD KKISLSTPLA DVPSCFSVTG
QKAYCPVNYD GTFHGAQQAR FALGNSYNIP AVRVLALNGL ENFIDFATKM GITTFTDPKN
YGLSLTLGGG EVVPYDMATA FGVFANQGIK QPLISILKVT DWKGKVLEEV NTKEIELTGD
RILTSDVTFL ISHILHDNNA RSAAFGESSF LNVRGHPEVS VKTGTTNDRR DNWTIGYTEY
ALTLSWVGNN DNSEMSGAVS GVSGASPIWN SIMRKVLDKA EEGFYNPEDD GHAWPKQPQG
VVGANVCATT GNLPDNPDSP GCPTRFEYFL KDKVGAGIET GTKDVQIDKT NGALAYPELP
PELIETQNRP FLLDPLGTLV CLDCPIASAS AKINYPLIAA PR
//
