PBPB_BUCAI
ID PBPB_BUCAI Reviewed; 760 AA.
AC P57296;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=BU200;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB12917.1; -; Genomic_DNA.
DR RefSeq; NP_240031.1; NC_002528.1.
DR RefSeq; WP_010895998.1; NC_002528.1.
DR AlphaFoldDB; P57296; -.
DR SMR; P57296; -.
DR STRING; 107806.10038882; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR EnsemblBacteria; BAB12917; BAB12917; BAB12917.
DR KEGG; buc:BU200; -.
DR PATRIC; fig|107806.10.peg.211; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_6; -.
DR OMA; VHGMGLA; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001806; 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..760
FT /note="Penicillin-binding protein 1B"
FT /id="PRO_0000083185"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..760
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 136..308
FT /note="Transglycosylase"
FT REGION 392..684
FT /note="Transpeptidase"
FT ACT_SITE 174
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 451
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 760 AA; 88003 MW; 00B2C5B51F6947D3 CRC64;
MFFNFKKYFL IKVFFFVLIL TLCYGLYLYV KINRFINGKV WNFPTSIYGR IVNLEPGNSY
SQKEVLHLLK STMYRKVDLV MLPGEYSIKN NTIEFIRRAF DFPDIREDEF HARLYFNKDT
LVKIKNIDNN HDFSFFRLEP KLIAMLKSPE AKKRMFIPRN QYPEMLVKTL LAIEDKYFYE
HDGIHLSSIG RAFLVNLMAG RTIQGGSTLT QQLIKNLFLT NTRSILRKIN EIYMALILDR
FYTKDRILEL YLNEVYLGQD GDEQIRGFPL ASIYYFGRPI NELNLEQYAL LVGMVKGASL
YSPWTNPNLA LKRRNLVLFL LYKQKYITRK IYKDLCKRSL NVQPKGNIIS SHPSFIQLVC
EEFHKKIYNP IKNFPGTKIF TTLDYTSQNA VEQAVKIEIP ILKRKKRLKD LEVAMIVIDR
FTGEVQALIG SSKPEFNGYN RALKTRRSIG SLSKPITYLT ALSQPEKYHL NTWISNYPLS
IKLDSGQYWT PKNNNFSFSK KVLLLDALIH SINIPTVNLS INIGLKKLVD SWLLLGISKK
YITPLPSISL GAINLTPFEI AQVFQIIGSG GYKSSLSSVR SIISDDGKVL YQNLPQSIHI
ESSEASYLTL YGMQQVVKSG TAKSLGTIFK EFSLAGKTGT TNNLVDNWFV GIDGKQIVIT
WIGRDNNHTT RLYSSSGAMQ IYKRYLQYQR PVPLVLKAPN NINMFYINNL GELFCKKNNQ
HNRMLPIWSI KNKKICNDKL SERFSIKKKK NFLFWLKNLF
