ID A0A8I0CZ36_9PSED Unreviewed; 765 AA.
AC A0A8I0CZ36;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN Name=pbpC {ECO:0000313|EMBL:MBC3294979.1};
GN ORFNames=HU722_0000765 {ECO:0000313|EMBL:QXH84051.1}, HU722_25990
GN {ECO:0000313|EMBL:MBC3294979.1};
OS Pseudomonas tritici.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2745518 {ECO:0000313|EMBL:MBC3294979.1, ECO:0000313|Proteomes:UP000615613};
RN [1] {ECO:0000313|EMBL:MBC3294979.1, ECO:0000313|Proteomes:UP000615613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWRI145 {ECO:0000313|EMBL:MBC3294979.1,
RC ECO:0000313|Proteomes:UP000615613};
RX PubMed=32752051;
RA Girard L., Lood C., Rokni-Zadeh H., van Noort V., Lavigne R., De Mot R.;
RT "Reliable Identification of Environmental Pseudomonas Isolates Using the
RT rpoD Gene.";
RL Microorganisms 8:E1166-E1166(2020).
RN [2] {ECO:0000313|EMBL:QXH84051.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SWRI145 {ECO:0000313|EMBL:QXH84051.1};
RA Girard L., Lood C., Vandamme P., Rokni-Zadeh H., van Noort V., Hofte M.,
RA Lavigne R., De Mot R.;
RT "Updating the genus Pseudomonas: Description of 43 new species and
RT partition of the Pseudomonas putida group.";
RL Submitted (JUN-2021) 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; JABWQF010000017; MBC3294979.1; -; Genomic_DNA.
DR EMBL; CP077084; QXH84051.1; -; Genomic_DNA.
DR RefSeq; WP_065891285.1; NZ_CP077084.1.
DR KEGG; ptrt:HU722_0000765; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000615613; Chromosome.
DR Proteomes; UP000615613; 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 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 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:UP000615613};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 54..202
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 297..517
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 674..756
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 765 AA; 84616 MW; AB7E9342E61963AE CRC64;
MKLPSLKRLT PLLAAAVLLA GLRLWPHAPL EQAVTSSRVV LADDGSLLRM TLADDGQYRL
WLPLERMSPS LVEALLLKED RNFYWHPGIN PPALLRAALA TYSGGQRQGG STLSMQLARR
LWDLNTRQVP GKLQQMALAL WLEARYSKHD ILEAYLNLAP MGGNIEGAEA ASRIYFGKSA
AQLSLSEALA LAVIPQQPGR RARFGPSLQN ARLRLMADWR ETYPQDPRND SLLDLPLEAR
NRQQIPFLAP HLSEQLLASQ PGNELNSTLN LPLQQLLERL ITGFIAERRS TGVENATAIL
IDSRDQSVKA LVGSADYLST SLHGQVNGVL SRRSPGSTLK PFLYGLALDQ GVIHPMSILK
DLPSNFGYFQ PENFDGSFVG PLTARDALIR SRNIPAVWLA SQVKSPSLYG LLQRAGIKGL
RDESHYGLAL ALGGGEMTPE ELARLYVMVA GDGRLRPLRY LQEQPQTTGA QLLTPQAAFM
VRDMLRRNPR PDGLPGRHWR TAWKTGTSWG FHDAWSAGLV GPYVLVVWVG NFDGRPNPAF
IGAKTAAPLF FRIADALPLA LPNVVIKPDK PPAGLVRIDI CAASGELPNR WCPQTRKTWY
IPGVSPIRVS NLHRPVLIDT RTGKAACPPF EAQYTREEVF EFWPSDVQRL YRAAGLPRRT
PPNVMKNCQP NRISDQSEAP QIRSPLTQVS YQLRLSQPQE SIPLNANAAS DAATLYWFAD
QTLIGQGPPQ TTLNWRPGKS GEYRLRVSDD QGRSASRGLR VEFVP
//
