PBPB_BUCBP
ID PBPB_BUCBP Reviewed; 741 AA.
AC Q89AR2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Penicillin-binding protein 1B;
DE Short=PBP-1b;
DE Short=PBP1b;
DE AltName: Full=Murein polymerase;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P02919};
DE AltName: Full=Peptidoglycan TGase;
DE AltName: Full=Peptidoglycan glycosyltransferase;
DE Includes:
DE RecName: Full=Penicillin-sensitive transpeptidase;
DE EC=3.4.16.4 {ECO:0000250|UniProtKB:P02919};
DE AltName: Full=DD-transpeptidase;
GN Name=mrcB; OrderedLocusNames=bbp_186;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits) (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:P02919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000250|UniProtKB:P02919};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
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DR EMBL; AE016826; AAO26918.1; -; Genomic_DNA.
DR RefSeq; WP_011091319.1; NC_004545.1.
DR AlphaFoldDB; Q89AR2; -.
DR SMR; Q89AR2; -.
DR STRING; 224915.bbp_186; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; AAO26918; AAO26918; bbp_186.
DR GeneID; 56470728; -.
DR KEGG; bab:bbp_186; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_6; -.
DR OMA; VHGMGLA; -.
DR OrthoDB; 652304at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011813; PBP_1b.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR028166; UB2H.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR Pfam; PF14814; UB2H; 1.
DR PIRSF; PIRSF002799; PBP_1b; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR02071; PBP_1b; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Carboxypeptidase; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Hydrolase; Membrane;
KW Multifunctional enzyme; Peptidoglycan synthesis; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..741
FT /note="Penicillin-binding protein 1B"
FT /id="PRO_0000083186"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..741
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 139..311
FT /note="Transglycosylase"
FT REGION 395..687
FT /note="Transpeptidase"
FT ACT_SITE 177
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 454
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 741 AA; 85683 MW; 950117AE79904004 CRC64;
MYPVNLKLSI KFLFYFFLYF LLIIIIYGVY LYFKINQVIH GKIWKFPISI YSRIVTLEPG
NNYSKKDIIA ILKSNRYKQV NFLTMPGEFL VKRNSLILIR RSFNFPEGFE DKISIKLLFD
KNKLVRIVHL SNNRNFSILR LDPQLIAMIY SPKGEKRLFV SQKNYPKALI QTLLTIEDKC
FYNHYGINFY SMFRAFFVNL ISGHSIQGGS TLTQQLVKNL FLTNIRSLWR KINEIYMALI
LDFQYSKEKI LELYLNEVYL GQDKNEQIRG FALASLYYFG RPINELRLDE CALLVGMVKG
ASLYNPWNNP VLTLNRRNLV LYVLFKHKVI NRTLYEKLKS KPLNIQSRGN IIWFRSAFVQ
IVEKEFQKKV GYYFQNFSGI KIFTTLDLIS QIAAENAIRH GIQQLKKKYK LQDLEASMVI
IDRFSGEIRG VLGSSNPNLL GYNRAIQAKR SIGSLSKPIT YLAALSQPEY FRLNTWIPDT
PIKIKMQNGK LWKPQNNNFE FVGKVMLIDA LKNSMNVPIV HLSMKLGLKK IVQTWIQLGL
SSNHIFKYPS IALGSINLTS MEVAKIFQVI SSGGNKANII SIRSVLSENN KLIYHSFPQS
KQVISAQASY LTLYAMQSVV SSGTAKHLGK FFKNMHLAGK TGTTNNLVDS WFVGIDGRQV
VIVWIGRDNN KTTKCYGSTG AMKIYHNYLK LNNPKPLLLI PPRDVYFLNI NKSGDFMCFR
SYSKYFRAIP VWIRNHNIFC T
