ID A0A095WM73_9BURK Unreviewed; 740 AA.
AC A0A095WM73;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=JL37_03850 {ECO:0000313|EMBL:KGD99703.1};
OS Achromobacter sp. RTa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1532557 {ECO:0000313|EMBL:KGD99703.1, ECO:0000313|Proteomes:UP000035841};
RN [1] {ECO:0000313|EMBL:KGD99703.1, ECO:0000313|Proteomes:UP000035841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RTa {ECO:0000313|EMBL:KGD99703.1,
RC ECO:0000313|Proteomes:UP000035841};
RA Prabhakaran M., Cougar B., Weirick T., Fathepure B.Z.;
RT "Genome sequences of the lignin degrading proteobacteria.";
RL Submitted (AUG-2014) 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:KGD99703.1}.
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DR EMBL; JPYO01000007; KGD99703.1; -; Genomic_DNA.
DR RefSeq; WP_043542146.1; NZ_JPYO01000007.1.
DR AlphaFoldDB; A0A095WM73; -.
DR eggNOG; COG4953; Bacteria.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000035841; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..241
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 328..587
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 649..733
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 740 AA; 79799 MW; 7672919C94D09236 CRC64;
MNAAVTPASG ATRARRWRRR GIFAASALFA LAALLFTLDR LYPLPPVDSG GAAVVVAADG
TPLRNYPSRD GIWRYPVKPG QVSERYLETL LTYEDRWFYW HPGVNPVALA RAGWQWATNR
RIVSGGSTLT MQVARLIDPE LAGKPSRSIF AKLRQAWRAV QLEMHYSKDE ILSLYLTHAP
MGGIVEGVEM GSRLWLGKPA RDLSPAEAAM LTALPQAPSR LRPDRHPEAA QAARDKVLDR
MVELGRWTPA EVADAKIEHV VAPPLRARWL APLAAQRLLQ EAAVKRPGSR RPGERPALVA
STLDADMQAS VERMLLDRVD GLPPKVSMAV LVMDNDTLEV KAYAGSADFS DDSRYSHVDM
VRGVRSPGST LKPFLYAQAL DEGLIHSESL LIDAPMSFGG YAPGNFQATF SGPVSVAQAL
QRSLNVPAVD LLDRVGPARF ASVMLAGGVW LRLPAGAQPN LSLILGGGGT TLEELVGAYR
ALARGGVSGR PRLRAEQPMV ESRMMSPGAA WIVRDILEGG GHPDRPFYQS GSPGRQLAWK
TGTSFGFRDA WAVGVTDRWT IGVWVGRPDG TPNPGFFGAN VAAPLLQDIV AALPEGVQQV
RVRPETVQAA VICWPLGYRL GSVPSGVCPE QRAAWILNET APPSFAGYAD ASQGPLRLQG
VAVGSVLRPV PGARQVALDV DVQGAEGEVW WMLDGRVVNH GAPDHPFKLV LAGDGRYTLT
VMDAQGRHDS VVFEIAGVTP
//
