ID A0A3B0MP09_9RHOB Unreviewed; 669 AA.
AC A0A3B0MP09;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpC {ECO:0000313|EMBL:SUZ32737.1};
GN ORFNames=ROE7235_02499 {ECO:0000313|EMBL:SUZ32737.1};
OS Roseibaca ekhonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Roseibaca.
OX NCBI_TaxID=254356 {ECO:0000313|EMBL:SUZ32737.1, ECO:0000313|Proteomes:UP000272908};
RN [1] {ECO:0000313|Proteomes:UP000272908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7235 {ECO:0000313|Proteomes:UP000272908};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (AUG-2018) 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}.
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DR EMBL; UIHC01000027; SUZ32737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0MP09; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000272908; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000272908}.
FT DOMAIN 53..221
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 298..505
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 587..666
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 195..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 71218 MW; 03D7C98BCB1EFA58 CRC64;
MKAVLGLVAA LVLTGWLALE RWVVATDLPP LNPPTSAEVL SEDGTLLRAY TVADGRWRLA
VDPARVDPTY RAMLLAYEDQ RFYTHMGVDP VALLRAVWQS VRAGHWVSGG STLTMQVARL
LEDGPTGTWT GKARQIRLAL ALERHLSKDA ILSLYLHLAP MGGNLEGLRA GARAWFGKDP
ARLTPAQSAL LIALPQSPTR RSPDRHPQAA RAARNRVLQR AVAARVLTRA EADAARSEHM
PDTRRPFPAL APHLSDRLVA ENPATGLHRT TIDAGLQAML EQTAQDTLRA LTPRAGLAIL
LADVQTGRVR AHIGGAYGVD MRAGFNDMTR AMRSPGSTLK PLVYGLAFSD GLAHPETLVN
DRPASFGGYA PQNFDGRFRG PVSVREALQL SLNLPVVEMT NTLGPARLMA ALRRAGVTTA
LNGPPGLAVA LGGVGVSLEG LVQLYAGIAR GGQTVTLQTA PGPVKTGPQI IAPEAAWHLG
QILARAPRPA HLPGWPLAFK TGTSYGHRDA WAVGFDGQHV AGVWIGRADG TPLPGTFGLD
AAAPVLFDVF AQLGARPVPL PPAPPRTLDV AHADLPPPLR RFGPQLAMDT DAPQLAFPPD
GAALRPVAGR VLARVDWGRA PFTWFANGAP VLTRSFERAA QLPLIGPGFV TLSVVDAMGR
AARVEVELQ
//
