ID A0A261VRQ6_9BORD Unreviewed; 721 AA.
AC A0A261VRQ6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=CAL24_12880 {ECO:0000313|EMBL:OZI76776.1};
OS Bordetella genomosp. 2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1983456 {ECO:0000313|EMBL:OZI76776.1, ECO:0000313|Proteomes:UP000215633};
RN [1] {ECO:0000313|EMBL:OZI76776.1, ECO:0000313|Proteomes:UP000215633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU8256 {ECO:0000313|EMBL:OZI76776.1,
RC ECO:0000313|Proteomes:UP000215633};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-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=2.4.1.129;
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:OZI76776.1}.
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DR EMBL; NEVT01000006; OZI76776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261VRQ6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000215633; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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 Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 50..230
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 309..531
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 630..714
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 721 AA; 77017 MW; CB36FE33C1AFE3A2 CRC64;
MLAARGRRRL ARLAGGFLAL AAALLALDWL YPLPPPGGGA AAVVVAADGT PLRTYPSRDG
VWRYPVTPGE VAPRYLEALL GYEDRWFYWH PGFNPVALAR AGWQWLAHGR IVSGGSTLTM
QVARLVDPGL AALPSRSPAA KLLQIARAVQ LEWHFSKDEI LGLYLAHAPM GGIVEGVEMG
ARLWLGKSAR DLSRAEAALL TALPQAPSRL RPDRHPQAAQ AARDKVLDRM AARGWSAAAI
ADAKLETVMA PPLRARWLAP LAAQRLMAGQ QRRGKRPAVV ASTLDADIQA TVERMLLDRV
DGLPPKVSMA ALAMDNDTLE IKAYAGSADF SDASRYAHVD MVRGVRSPGS TLKPFLYAQA
LDDGLIHSES LLLDAPLSFG GYAPGNFQAA FSGPVSVAQA LQRSLNVPAV DLLDRVGPAR
FSAAMLAGGV RLRMPDGAAP NLSLILGGAG TTLEELVGAY RALARDGLAG RPRLAPGQPR
VESRMMSAGA AWIVRDILEG GGHPDRPLWQ DGAPGRRLAW KTGTSFGFRD AWALGVTDRW
TIGVWVGRPD GTPNPGFFGA NVAAPLLRDI AATLPAGTPQ PRRRPASVQP VIACWPQGWR
QGGMPAQPCS QPRSAWALDQ TVPPTFAGYA DAARGPLRLQ GVADGSVLRP VPGRQEVVLD
VSVQGARGEV WWMLDGRVKQ RGEPSAPLQL ALVHNGRYTL TAMDAQGRYD RVVFEISGVT
P
//
