ID A0A0Q5YPQ9_9BURK Unreviewed; 675 AA.
AC A0A0Q5YPQ9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ASG30_17360 {ECO:0000313|EMBL:KQT07600.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT07600.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT07600.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT07600.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT07600.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT07600.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQT07600.1}.
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DR EMBL; LMQL01000015; KQT07600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5YPQ9; -.
DR STRING; 1736365.ASG30_17360; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051173; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051173};
KW Transferase {ECO:0000313|EMBL:KQT07600.1}.
FT DOMAIN 73..246
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 351..582
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 675 AA; 75065 MW; 7309C57493DE7668 CRC64;
MNPTMGRFLD AIRAGWTRLW GAVRRHPWRT ALVPPGLVLL YVLALLPFTP GIGNLRKAKV
EAPAVLVSAD NVVLASYKRV NREWVPLDKV APAVVQALIH TEDHRFWDHH GIDWYRTAAS
AWHTLKGRRQ GGSTLTQQLA RNLYPEEIGR SPTVHRKVKE AITALKIEAV YSKKEILETY
LNTVPFLYNA FGIEMAARTY FDKPASELDV LESATLIGML KGTSYYNPVL NPERARERRN
VVLDQMAKHG SLPAERAEQL AKRPLKIDFE RQQEPLGPAP HVAQHVRKWL IAWADRNGYD
IHSDGLVVRS TLDTRLQRAA NESVTRQLSQ LQPLADRRRK AGQDPALLQA GFLALDPRNG
HVLAWVGSSD FARDQFDHVS QARRQPGSTF KPFVYGAAFL DGFGPNDTLI DQPVVLRGAN
GETWSPRDST PPTNAPWTLR AGLVFSRNSI TAQLMERVGP QKVAKLAQAM GVRESRLDAV
PSLALGTSPV TLREMVSAYG TLANNGRWVE PLLVLRIEDS EGKVLDAFVP PRSAEAMPKA
KALMLVNAMR GVVDEGTGAA IRSRYGIQAD VAGKTGTTQD NADGWFILMH PHMVAGAWVG
FNDPSITMPD AWGPGARSAL PIVGDYFQQS VRNRWVDTKA EWDIPRPRPK PKQPEGDPLE
RLVNDVIDRL FKILQ
//
