ID A0A085V909_PSESX Unreviewed; 774 AA.
AC A0A085V909;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=IV01_22620 {ECO:0000313|EMBL:KFE51922.1};
OS Pseudomonas syringae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=317 {ECO:0000313|EMBL:KFE51922.1, ECO:0000313|Proteomes:UP000028631};
RN [1] {ECO:0000313|EMBL:KFE51922.1, ECO:0000313|Proteomes:UP000028631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAW0119 {ECO:0000313|EMBL:KFE51922.1,
RC ECO:0000313|Proteomes:UP000028631};
RA Baltrus D.A., Berge O., Morris C.;
RT "Draft Genome Sequences of Environmental Pseudomonas syringae strains.";
RL Submitted (JUL-2014) 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:KFE51922.1}.
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DR EMBL; JPQU01000078; KFE51922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085V909; -.
DR PATRIC; fig|317.175.peg.4713; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000028631; 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: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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 54..220
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 296..412
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 689..769
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 774 AA; 84978 MW; 004C6A819ED4DD0F CRC64;
MYRICRWLVA GMLLLITLLW LADRLWPLPL PKDDLARVVL AEDGTPLWRF ADANGVWRYP
VSSAQVSPYY IEALLTYEDR WFYSHPGVNP LSLVRASWQN LSGARVISGG STLSMQVARL
LDPHSRTLHG KARQLWRTLQ LEWHLSKDEI LAIYLNRAPF GGTLQGVAAA SWAYLGKSPQ
QLTRAEAALL AVLPQAPSRL RPDRHPQRAQ AARDKVLRRL AEFQVWPQIA VNEALEEPLL
LAPRQEPSLA PLLARRLNRP DSPPLIRTTL DAGLQRRLED LLLGWRARLP ERTSAAILVV
EAQNMAVRAY VGSVDINDAK RFGHVDMISA LRSPGSTLKP FLYGLSMDAG LIHSESLMQD
VPRRYGDYRP GNFAAGFSGA VAASSALSMS LNLPAVQLLE AYGPKRFAAE LRNGGVPLTL
PPLAEPNLAM ILGGVGSRLD ELVGGYSAFA RGGRSADIRL QPDAPLRDRH MMSPGAAWII
RKILSGQSRP DLDPHAELVQ RPQLAWKTGT SYGFRDAWAI GVGPRFLVGV WIGRPDGTPV
PGQFGLASAA PLMLQVHDVL ANRDSQRGIA APIQPVPGNV GVAAICWPLG QPMSKSDPNC
RRQRFAWTLD GTTPPTLQAL DQPLGLGLLE KIWVNEKGLR VASHCLGAQA RDIALWPAPL
EPWLLRSERR EARLPPIDPD CPPQGLSLAT PLSIVGVREG DHLRLPAGSR QALRLKLSAL
GGSGRRWWFI DGVPMADTQS QDTFNPTLSR LGRVELSVLD ESGQTARLVF EVVD
//
