ID A0A117UWD3_9SPHN Unreviewed; 704 AA.
AC A0A117UWD3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=AQZ49_20810 {ECO:0000313|EMBL:KUR72043.1};
OS Novosphingobium sp. FSW06-99.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR72043.1, ECO:0000313|Proteomes:UP000061032};
RN [1] {ECO:0000313|EMBL:KUR72043.1, ECO:0000313|Proteomes:UP000061032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR72043.1,
RC ECO:0000313|Proteomes:UP000061032};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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:KUR72043.1}.
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DR EMBL; LLZQ01000035; KUR72043.1; -; Genomic_DNA.
DR RefSeq; WP_067620657.1; NZ_KQ954269.1.
DR AlphaFoldDB; A0A117UWD3; -.
DR STRING; 1739113.AQZ49_20810; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000061032; 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000061032};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..252
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 338..561
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 603..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 75417 MW; 9154DA91AF9D5226 CRC64;
MAPRDNSRRR KSGGEGPRSG SFLGRLVKGL VIWSCAVVLL AAIGLTAAVL VTARSLPSYD
RLKSSQTGHM IVVRADDGSE IVTLGPSYGK WIPISRMPRV MQDAMISVED RRFHDHWGVD
PIGIARSVMV RVQKGHWRQG GSTITQQLAR NTFLNSSRTF DRKIREIVIA LALETKFSKD
QILELYLNKV YFGGGAYGVD SAARKFFGHS GEQLSLGEAS IIAGLVKAPS HYSPTADAKA
AVDRAQVVLE TMEDAGAITP AEEKAVDLKS VKMAEEAGQN SARYFTDWVL PQLDQILPDN
DQQIEVWTTL DPAAQRAATE AIQTNAPKGA QGALVSVDRD GAVLAMVGGT DYVTSNYNRA
TNAVRQPGSS WKLFVYLAAL EAGYKPDDKV VDEPVTIDGW TPRDSGGKYA GQIDVRTAFA
YSKNTVAAQL GNEVGFGAVA NMARRFGIST PINTLPSMVL GTNDVRMLDM VRAFSEISAK
GATVIPYGIR KVTTTEGEVL YSHRPDPAQQ LVPDYVAAGI TDLLQTAVAI GTGRAAQIGR
PVAGKTGTTS SNKDGWFLGF SSGITTGVWM GRDDAKPVPG LQGGTAPARA FAAYMRVATA
KRPPEKFQTE LKLPTQQLEP DDETLQNNPD SYFYVDPNGN IANHQGADGT AVAPAPARPR
DDTTPVQEDG GAAANDDFLD RATGRPAGSA HRPPPTGRAT PHPN
//
