ID B3PU34_RHIE6 Unreviewed; 727 AA.
AC B3PU34;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbp {ECO:0000313|EMBL:ACE90338.1};
GN OrderedLocusNames=RHECIAT_CH0001357 {ECO:0000313|EMBL:ACE90338.1};
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE90338.1, ECO:0000313|Proteomes:UP000008817};
RN [1] {ECO:0000313|EMBL:ACE90338.1, ECO:0000313|Proteomes:UP000008817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE90338.1,
RC 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; CP001074; ACE90338.1; -; Genomic_DNA.
DR AlphaFoldDB; B3PU34; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; rec:RHECIAT_CH0001357; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008817; Chromosome.
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: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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..296
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 384..651
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 79925 MW; B08E676ABF4DBBA5 CRC64;
MQDPDNPEKG PENGAEKQAA DTGRRPAKSR HILLRIDSWI DSTVWNAGFR AAEIWEDTTI
FFRRFRVRGW KRIVFELAGE GLTLGTVGAV LMLVLAQPAF EATKEDWRNR GDFAVTFTDR
YGNVIGHRGV IHQNSVPIDE LPDSLIKSVL ATEDRRFFDH FGIDAIGLFR AMVTNAQAGE
VVQGGSTLTQ QLAKNLFLSN ERSIDRKVTE AFLALWLEAN LSKKQILSTY LDRAYMGGGT
FGAAAAAQFY FGKNITDVNL AESAMLAGLF KAPAKYAPHV NLPAARARAN EVLTNLVQSG
LMTEGQVIAA RRNPATVVDR NEVESPDFFL DWAFDEVQRL SPRFHQHSLI VRTTIDMGIQ
KAAEDSVETS LREYGEAYHA KQGAMVMIEN GGAVRAMVGG RDYGESQFNR ATKALRQPGS
SFKVYTYALA MESGMTPQTT IVDAPISWGN WSPHNYANRY VGRITLETAI AQSINTVPVR
LAKEKLGIQP IRAMAKNLGV ETPIRDDVTI PIGTSEVTVL DQATAYATFP AGGYQSRRHG
ISQILDYEGD VLYDFDRDEP AAKRVLSEQA DAYMNQMLSR VPYVGTARKA ALDNGVLTAG
KTGTTQAYRD AWFVGFTGNY TCAVWFGNDD YTSTNNMTGG SLPAMTFKRA MDYAHQGVTL
RAIPGVENPP PSEKDVAKTA ATKPQDGLPQ LIRPRMLSVE STTILKDLGK RLKEAAPLTP
QKVASAE
//
