ID A0A2I0CMI0_9PSED Unreviewed; 772 AA.
AC A0A2I0CMI0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=CW360_13715 {ECO:0000313|EMBL:PKF70355.1};
OS Pseudomonas pharmacofabricae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1905276 {ECO:0000313|EMBL:PKF70355.1, ECO:0000313|Proteomes:UP000242861};
RN [1] {ECO:0000313|Proteomes:UP000242861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZYSR67-Z {ECO:0000313|Proteomes:UP000242861};
RA Yu X.-Y.;
RL Submitted (DEC-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}.
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:PKF70355.1}.
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DR EMBL; PIYS01000027; PKF70355.1; -; Genomic_DNA.
DR RefSeq; WP_101194080.1; NZ_PIYS01000027.1.
DR AlphaFoldDB; A0A2I0CMI0; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000242861; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000242861};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 55..221
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 326..516
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 686..764
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 772 AA; 84894 MW; 2C6C41BFFE32F466 CRC64;
MLWLKRRPWL LAPLGLLALL WLADRLWPLP LPGDDLARVV LAEDGTPLWR FADQDGVWRY
PVTAQEVSPY YLEALLGYED RWFYQHPGVN PLALARAAWQ NARAGRVLSG GSTLSMQVAR
LLDPHARSYA GKLQQLWRTL QLEWHLSKEE ILTLYLNRAP FGGTLQGVAA ASWAYLGKPP
SQLTRAEAAL LAVLPQAPSR LRPDRHAARA QAARDKVLRR LLASGQWPAE AVRDALQEQL
FLAPRREPQL APLLARRLNR GDTPAHLRTT LDAALQQRLE DLLLGWRGRL PARTSAALLV
VEHDSMAVRA YLGSLDFSDD QRFGHVDMVR ALRSPGSTLK PFLYGLALDA GLIHSESLLQ
DVPRRYGDYR PGNFAAGFSG PVAASTALST SLNLPAVQLL EAYGAKRFAG ELRAAGLPLY
LPAGAEPNLA LILGGAGARL EQLVGAYSAL ARDGMAAEVR LQPQQALRER RLLSPGSAWI
VRRILSGQAR PDRDPRAALS QRAPLAWKTG TSYGFRDAWA IGVGPRYSIG VWIGRPDGTP
VQGQFGLASA APLLLQVHDL LENRERQRGR VAPADPQPDS VGVAAICWPL GQVLPRQHAD
CRRQRFAWTL NGTVPPTLLA ADQPLGLGLR EHFWVDEQGR RVARHCARAQ PAERLLWPAP
LEPWLPRRER RSARLPAPSA DCPPSAQAQA PLSIVGVRQG DRLRRLQAGA LNLQVSALGG
SGRYWWFLDG QPLAVLGDGR EQALSLPRLG GYQLSLLDDS GQVALLDFEL RD
//
