ID A0A2D2M272_9PSED Unreviewed; 784 AA.
AC A0A2D2M272;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=CS390_03105 {ECO:0000313|EMBL:ATR81609.1};
OS Pseudomonas sp. HLS-6.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2049589 {ECO:0000313|EMBL:ATR81609.1, ECO:0000313|Proteomes:UP000230810};
RN [1] {ECO:0000313|EMBL:ATR81609.1, ECO:0000313|Proteomes:UP000230810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLS-6 {ECO:0000313|EMBL:ATR81609.1,
RC ECO:0000313|Proteomes:UP000230810};
RA Hu Y., Zhang T., Lei D., Yao S., Lin K., Chen X., Cui C.;
RT "Complete genome of Pseudomonas sp. HSL-6, a multiple-antibiotic-resistant
RT bacteria isolated from drinking water source in East China.";
RL Submitted (OCT-2017) 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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
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}.
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DR EMBL; CP024478; ATR81609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D2M272; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000230810; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR FunFam; 1.10.3810.10:FF:000006; Penicillin-binding protein 1C; 1.
DR FunFam; 3.40.710.10:FF:000021; Penicillin-binding protein 1C; 1.
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; IPR050396; Glycosyltr_51/Transpeptidase.
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 NCBIfam; NF008414; PRK11240.1; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
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:UP000230810};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..230
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 307..425
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 697..780
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 784 AA; 85715 MW; E0AE4EBEA3C50D71 CRC64;
MFSVVRPDSR TGRWLAGIAA SGLLLCALLW LADRIWPLPL PADDLARVVL AEDGTPLWRF
ADANGVWRYP ITPEQVSPLY LQALLTYEDR WFYRHPGVNP LALGRAVWQN LQGGRVVSGG
STLSMQVARL LDPHARTLPG KLRQLWRTAQ LEWHLSKDEI LQIYLNRAPF GGTLQGVAAA
SWAYLGKSPQ QLTPADAALL AVLPQAPSRL RPDRHPQRAQ AARDKVLQRL AEYRVWPEQQ
VAEAAQEPLL LAPRQEPTLA PLLARRLNRP GSPPLIRTTL DAALQRRLED LLLGWRARLP
ERTSAAILVV ESQTMAVRAY LGSVDLGDTR RFGHVDMISA LRSPGSTLKP FLFGMALDEG
LIHSESLLQD VPRRYGDYRP GNFSQGFSGP VSASSALALS LNLPAVQLLE AYGPKRFAAQ
MRQGGMPLTL PPLAEPNLSL ILGGAGSRLE DLVSGYSAFA RNGMSAALRL QPDDPLLERR
LLSPGAAWIT RRILSGQARP DLDPHAELVQ RPQLAWKTGT SYGFRDAWSI GVGPRYLIGI
WIGRPDGTPV PGQFGLASAA PLMLQVHDVL SNRDSQRGIT APVAAVPANV GVAAICWPLG
QPMARQDDNC RRQRFAWTLD GTTPPTLQAL DQPLSVGLLE KVWVNDQGLR VDAACPGAHA
RDIALWPAPL EPWLPRVERR EARLPAIDPR CPPKVPDATA PLSIVGVRNG DQLRRPATSR
DALQLKVSAL GGSGQRWWFL NGAPVGETAA QDSLTVSFEQ AGRYELSALD ASGQTARIEF
QVND
//
