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Database: UniProt
Entry: A0A0G1XPZ3_9BACT
LinkDB: A0A0G1XPZ3_9BACT
Original site: A0A0G1XPZ3_9BACT 
ID   A0A0G1XPZ3_9BACT        Unreviewed;       646 AA.
AC   A0A0G1XPZ3;
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=UY77_C0009G0013 {ECO:0000313|EMBL:KKW32945.1};
OS   Candidatus Uhrbacteria bacterium GW2011_GWA2_53_10.
OC   Bacteria; Candidatus Uhrbacteria.
OX   NCBI_TaxID=1618980 {ECO:0000313|EMBL:KKW32945.1, ECO:0000313|Proteomes:UP000034711};
RN   [1] {ECO:0000313|EMBL:KKW32945.1, ECO:0000313|Proteomes:UP000034711}
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:KKW32945.1}.
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DR   EMBL; LCRI01000009; KKW32945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1XPZ3; -.
DR   PATRIC; fig|1618980.3.peg.206; -.
DR   Proteomes; UP000034711; 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        36..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          116..269
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          359..635
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   646 AA;  71032 MW;  830D30F41405A5A9 CRC64;
     MASLSSHRGY TWRRSRSSSE HRKGSGRFNK EWAKNAVLLG IAALFAGSIG ILGVFAYVSR
     DLPDPNALTE RLVKQSTKIY DRTGEHLLYE IYSDENRTLV KMQEGFCKDK PLEETDHAGI
     PLLAIQATIA AEDRVFCAHH GFTVKGLARA VLFGGSRGGG STLTQQLVKN AVLSNEKTLT
     RKAKELILSI ELERRYSKDE ILQIYFNEIP YGSTYYGIQA AAQNYFRKTV NGLSLAEVAT
     LAALPKSPTT YLNNPDLLHA RRDWILNEMV EMGFVTAEAA SEAKAQETPV KVKVTNIQAP
     HFVFYVKEAL EERYGRRTVE EGGLKVLTSL NFNLQTAAEE AVTSGVDTRG KQYQFTNASL
     VAMDPKTGQV LAMVGSKDYF DDDIDGQVNV SLRPRQPGSS FKPIVYAKAF ASSYTPNTIL
     WDVKTDFPTP VGIYAPNNYD LKERGPVRAR EALQGSLNIP AVEMLYLVGI DPTLNFAESL
     GYTTFGNRSN FGLAIVLGGG EVKLLEHVNA YATFANAGVH FDPINILKVE DASGHILEEW
     KAMDGRKVVE PNAAAMISNV LSDNSARSYV FGPTSYLQLG ARPVAAKTGT TNDYHDAWTV
     GYTPSLAAGV WVGNNNYDAM KRGADGSIIA APIWNQRHRI HPCHLP
//
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