ID A0A0G1XE05_9BACT Unreviewed; 939 AA.
AC A0A0G1XE05;
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=UY73_C0015G0006 {ECO:0000313|EMBL:KKW29518.1};
OS Parcubacteria group bacterium GW2011_GWA2_52_8.
OC Bacteria.
OX NCBI_TaxID=1618857 {ECO:0000313|EMBL:KKW29518.1, ECO:0000313|Proteomes:UP000033838};
RN [1] {ECO:0000313|EMBL:KKW29518.1, ECO:0000313|Proteomes:UP000033838}
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:KKW29518.1}.
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DR EMBL; LCRE01000015; KKW29518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1XE05; -.
DR PATRIC; fig|1618857.3.peg.194; -.
DR Proteomes; UP000033838; 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 64..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..288
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 379..658
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 939 AA; 104027 MW; 5C0F89EB505498F3 CRC64;
MNDYSRGWRA SRTPDFRRIE RRTDNFSRPP KKSLKFWAYL AIVWRFIKNL SKRFWRVRGW
WKKLVIMGSA GALVLFIFFG LLFVYYSFAL PSPDKLADRV VPESTKIMDR NGKLLYEIHG
EAKRTLIPLD QIPQHAKDAV IAIEDKNFYS HGGVSFTGIL RAALVNVFSG SLRQGGSTIT
QLFVRNAVLT REKTFARKFK EIVLSLQIEK KYGKDEILQL FFNEIPYGSN AYGIEAASQT
FFSKSAKNLS LLESAYLAAL PKGPTYYSPY GPRRDELDAR ADTVLQLMYE QGYITEAERN
QAQNTAVEFR VIGQGILAPH FVLYIQDLLA QKYGELSLQE GGLKVTTSLD LDLQTIAEEA
VTKQGEINEQ NYKATNAALV SIDPRTGEIL AMVGSRDYFN EEIDGAVNVA LRPRQPGSSF
KPYVYSTAFK EGMSPATMLF DVVTNFGEFG GKDYTPQDYD GKQRGPISIR SALQGSLNIP
AVKTVLLVSV EDSIDTAEAM GITTLKDRSR FGPSLVLGGA EVKLLEHTAA YGTFATGGIK
HDTVAILKVE DKTGRVLEEH ASSGGREVLN AQIAYQINNV LSDNESRIYI FGRNNRLTLP
GRPAAAKTGT TQENRDNWVI GYTPSLVTGV WVGNNNNDEM AERAFGSSTT APIWQEFMRR
ALEGKPVEEF TRPEGIAEIV VDSLTGKLPT AYSPSTKTEV FASFNAPTES DDVHFAGYNV
LHSEKPDDPD WEEPVKAWAL QNGYLWEPDD GQSADPTIEL SLTAPAKITG APWSARIEAT
GNQEVKELEL FLDNYLLAAS ANSTLDYESA TLHVSGRHQL TAQVRTRDNK INQKSVTVEF
QNGPNLLLLT PRDNQEVGLP TNIVLESNIN IAAENAKFRL RNAGGDESEI AGNITKQQLG
QIYHYTLNWA SGQKPAKGSY QLWGGISGES SAAATIKIP
//
