ID A0A549T5E1_9HYPH Unreviewed; 694 AA.
AC A0A549T5E1;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
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:TRL37074.1};
GN ORFNames=FNA46_16635 {ECO:0000313|EMBL:TRL37074.1};
OS Rhizobium straminoryzae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=1387186 {ECO:0000313|EMBL:TRL37074.1, ECO:0000313|Proteomes:UP000316801};
RN [1] {ECO:0000313|EMBL:TRL37074.1, ECO:0000313|Proteomes:UP000316801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM12 {ECO:0000313|EMBL:TRL37074.1,
RC ECO:0000313|Proteomes:UP000316801};
RA Tani A.;
RT "Ln-dependent methylotrophs.";
RL Submitted (JUL-2019) 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:TRL37074.1}.
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DR EMBL; VJMG01000047; TRL37074.1; -; Genomic_DNA.
DR RefSeq; WP_143126323.1; NZ_VJMG01000047.1.
DR AlphaFoldDB; A0A549T5E1; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000316801; 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:UP000316801};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..694
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021902946"
FT DOMAIN 61..227
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 305..532
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 605..691
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 694 AA; 74233 MW; F20DC02C5637A8B9 CRC64;
MRRWRLAAAG AAGLVLLATA GLVALDAADR AFPPPLEAAS EISPEVFDAE GRLLRAFATR
DGLWRLKTTA ADVDPQFLRM LVAYEDRRFY AHGGVDPYAV LRAAGQLLTS GRIVSGASTL
SMQVARLIEP RDSRSLLAKL KQMARAVQIE RRLGKGEILD LYLTLAPYGG NLEGVRAASL
AYFGKEPKRL SVAEAALLVA LPQSPEARRP DRFPEVARAA RQRVLGRETV ATAVGEGEAE
RAALAGVPRE RRQLPALAAH LAEAAVRLKP DERRHVTTLL KPIQQGLEAV AAAAVSGLPP
KTSLAMVMAD ATTGAIVAEV GAADYFDVAR SGWIDMTRVP RSPGSTLKPF IYGLAFEDGL
VAQETIIEDR PADFSGYRPR NFDMRYQGDV SVREALQLSL NVPAVRLLEG VGPAKLMVRF
RRAEVRPMLP AGEAPGLAIG LGGVGLTLKD LVQLYAGLAN QGFPVLLGDG IRDQPRRLAA
EPLLDPVAVW NVTDVLSDVL PPQGARKLGL AYKTGTSYGY RDAWSVGYDG RYVLGVWVGR
PDNGAVPGIT GYGTAAPLLF EAFARSGVAI SPHPPPPSGA QRLALSDLPI GQRRYAVTAS
GLVRSSTREA APQIVYPPEG ARVDLGARAG QEIAPLVLKL QGGRAPFRWL ANGKPLSDLS
RKRISEWQPD GAGYSTLTVI DAVGRAATVR VFIE
//
