PBPB_HAEIN
ID PBPB_HAEIN Reviewed; 781 AA.
AC P45345;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
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; Synonyms=ponB; OrderedLocusNames=HI_1725;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 inner membrane {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; L42023; AAC23371.1; -; Genomic_DNA.
DR PIR; D64138; D64138.
DR RefSeq; NP_439866.1; NC_000907.1.
DR RefSeq; WP_005694212.1; NC_000907.1.
DR AlphaFoldDB; P45345; -.
DR SMR; P45345; -.
DR STRING; 71421.HI_1725; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PRIDE; P45345; -.
DR EnsemblBacteria; AAC23371; AAC23371; HI_1725.
DR KEGG; hin:HI_1725; -.
DR PATRIC; fig|71421.8.peg.1804; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_6; -.
DR OMA; VHGMGLA; -.
DR PhylomeDB; P45345; -.
DR BioCyc; HINF71421:G1GJ1-1740-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000579; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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 inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW Peptidoglycan synthesis; Protease; Reference proteome; Transferase.
FT CHAIN 1..781
FT /note="Penicillin-binding protein 1B"
FT /id="PRO_0000083184"
FT REGION 151..322
FT /note="Transglycosylase"
FT REGION 415..702
FT /note="Transpeptidase"
FT REGION 749..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 466
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 781 AA; 88257 MW; 769CD5DE9A6E488E CRC64;
MTSQHSAKKS SKNTPKNNRT FKGFLLKFSF TALVLTIFYG GYLDWQIRSK MDGQIWHLPA
EVYSRLESVK IADNLAFDEV IQILLDNEYR QTTMVAAPGD FKLEDDSIVV LRRAFPFPDK
AEPQRVLRLR FSHNKLSRIE DLVTVKTVDE FRLAPKLIAM LQSDNEDRLA IPLQNYPRLL
IDTLILTEDR RFYEHNGINP VGILRALIAN IRAGQTVQGG STLTQQLVKN LFLSRERTIT
RKANEALMSL VLDWRYDKNR ILETYLNEIY LGQNGDTQIH GFELASQFYF GRSIREISLD
QIALLVGMVK GPSLYNPWRN PQNALERRNI VLRLMLEHKM IGDELYQLLS QRPLGVQKKG
QISRKYPAFI QTLQADLRRK LGEHKISSLL GARIFSTMDL KQQAQAENAV GNTVSQLQLK
MKNPHLEGAM IITDYRTGEI RAVVGGLQTQ YAGFNRALMA KRQIGSLVKP SIYLTALSNP
EQFRLNTPIN NQPITINVKG SPPWQPRNYD KKYSDSVMLM DALARSLNIP TVNIGMKVGL
SKVIDTQKAM GWDNVEIPKV PAMLLGSYTI SPYDVTKLYQ TLANQGGRIA LTTVDSIADR
QGNLIFQHDK SAKQVVPQEA AFQTLFAMQQ TVERGTARSL QKDYADLHLA GKTGTTNESR
DTWFVGIDGK NISTVWLGRD DNGETKLTGA SGALQIYKDY LNRTNIEKLA ITPPTTVKWV
GINQYGDWDC ESYRTIPIWL NNGQNFCGET SSPSLTPTTE TETPPQESLW DVLDNPNPPA
Q
