ID A0A0G0U1W5_9BACT Unreviewed; 744 AA.
AC A0A0G0U1W5;
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=UT79_C0002G0167 {ECO:0000313|EMBL:KKR44127.1};
OS Candidatus Moranbacteria bacterium GW2011_GWC2_40_12.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618699 {ECO:0000313|EMBL:KKR44127.1, ECO:0000313|Proteomes:UP000034716};
RN [1] {ECO:0000313|EMBL:KKR44127.1, ECO:0000313|Proteomes:UP000034716}
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:KKR44127.1}.
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DR EMBL; LBYD01000002; KKR44127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0U1W5; -.
DR PATRIC; fig|1618699.3.peg.661; -.
DR Proteomes; UP000034716; 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 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 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 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..251
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 342..621
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 697..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 83073 MW; 85E51B49BEAE9641 CRC64;
MKNELVDNTK NALKKPKKKR KWLRRIFKIF VWCFVAGLLL AIGVFAYYAK DLPSPGKLNK
RQVVESTKIY DRTGEHLLYE IHGEEKRTTI PLKDMGEVIK AATLSAEDQS FYQHHGIYFK
SIARAAIYDL IGRQVSQGGS TISQQLIKNT VLTNEKTFTR KVKEVILSVE LEQRFSKDEI
LEMYLNEIPY GSNAYGVQAA AQTFFGKDAK SLTLAEAALL ASLPKAPTYY SPYGSNTDDL
RGRQEYVLDQ MAKLGYITRE EAEGAKEIDI ISEVRPFQES IQAPHFVMYV KDLLVNKYGE
QQVEEGGMKV FTTLDWDKQQ IADEAVKKGV ANNSKYKASN AALVAIDPKT GQILAMVGSR
DYFDKTIDGN VNVAIRDRQP GSSFKPYVYA TAFKKGYTPN TMLFDVETNF GTKEKPYAPQ
NYSNNFSGPV KMKEALARSL NIPAVKTLYL AGVQNSVNTA QSMGITTLKN PSRYGLALVL
GGGEVKLVDH VNAFGTFATG GVRHDKTAIL KITYSQGNLL DEYKNSAGEK VLDQDICAKI
DSILSDNSLR SSVFGSNSPL RFDSRPVAVK TGTTNEWRDA WTVGYAPNLV AGVWAGNNNN
APMAQGSDGV YVAAPIWREF MDRAFSNMAI EKFPEVKDEK TGKAILDGTV QGEEKEVTVC
KISDGKYCLA NDNCPDNEKR RHKKFFSAHS ILYWIDKDNP RGDAPKQPQK DPQFSAWEKG
VQKWAEKKEL DVQENVEECK SSDF
//
