ID B3Q0Z9_RHIE6 Unreviewed; 693 AA.
AC B3Q0Z9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=RHECIAT_PA0000009 {ECO:0000313|EMBL:ACE93355.1};
OS Rhizobium etli (strain CIAT 652).
OG Plasmid pA {ECO:0000313|EMBL:ACE93355.1,
OG ECO:0000313|Proteomes:UP000008817}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE93355.1, ECO:0000313|Proteomes:UP000008817};
RN [1] {ECO:0000313|EMBL:ACE93355.1, ECO:0000313|Proteomes:UP000008817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE93355.1,
RC ECO:0000313|Proteomes:UP000008817};
RC PLASMID=Plasmid pA {ECO:0000313|Proteomes:UP000008817};
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) 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; CP001075; ACE93355.1; -; Genomic_DNA.
DR AlphaFoldDB; B3Q0Z9; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; rec:RHECIAT_PA0000009; -.
DR HOGENOM; CLU_006354_7_3_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008817; Plasmid pA.
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 Glycosyltransferase {ECO:0000313|EMBL:ACE93355.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Plasmid {ECO:0000313|EMBL:ACE93355.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ACE93355.1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..693
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002794635"
FT DOMAIN 51..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..689
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 693 AA; 74402 MW; 5FC4D47B284B4C2B CRC64;
MRLWRKFAIG SAAGIVVAGA ALLALDAADK AFPPPLDKAG MVSPEVLDAD GQLLRAFATG
EGRWRLKTTV ADVDPQFLRM LVAYEDQRFY DHGGVDAWAL GRASLQFVRN GRIVSGASTL
SMQVARLIEP RAERSFSAKL LQLVRAVQIE RRLSKEEILD LYLTHAPFGG NLEGVRAASL
AYFGKEPRRL MVAEAALLVA LPQLPERRRP DRNLQAAQEA RKRVLDRAAV AEAVGAGEAE
RAEAVAVPMR RMQLPALAAH VAEAALRKEP DVLKHRTTLK KQVQQGLEAV ARAAAMKLGP
KLSLAMVMAD AETGAIVGEV GSADYFDASR SGWIDMTRVN RSPGSTLKPF IYGLAFEQGL
VSQETIIEDR PADFFGYRPR NFDMSYQGDV TVREALQLSL NVPAVKLLDA VGPSRLLVRF
RRADVRPALP PNETPGLAIG LGGVGITLKD LVQLYTALAD RGRPARLGDG ITGTPEKLDG
EPLLEPVAVW NVADILSGVI PPAGAPQRGI AYKTGTSYGY RDAWSVGYDG RYVLGVWVGR
PDNSAVPGLT GYGTAAPILF EAFAKSGIAT TPLPRPPAGA VRIAQSELPI SQRRFALNAS
GLLVASGREP APQIVYPPEG AHIDLGAKGG DLSPLMLKLQ GGRAPFRWLA NGKPLPDLSR
RRTQQWQPDG GGYSKLTVID SAGRAASVGV FID
//
