PBPB_VIBCH
ID PBPB_VIBCH Reviewed; 777 AA.
AC Q9KUC0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=VC_0602;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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 inner membrane {ECO:0000250}; Single-pass
CC type II 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; AE003852; AAF93769.1; -; Genomic_DNA.
DR PIR; A82303; A82303.
DR RefSeq; NP_230252.1; NC_002505.1.
DR RefSeq; WP_000197283.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KUC0; -.
DR SMR; Q9KUC0; -.
DR STRING; 243277.VC_0602; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR DNASU; 2615390; -.
DR EnsemblBacteria; AAF93769; AAF93769; VC_0602.
DR KEGG; vch:VC_0602; -.
DR PATRIC; fig|243277.26.peg.572; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_6; -.
DR OMA; VHGMGLA; -.
DR BioCyc; VCHO:VC0602-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000584; Chromosome 1.
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; 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; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..777
FT /note="Penicillin-binding protein 1B"
FT /id="PRO_0000083187"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..52
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..777
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 162..334
FT /note="Transglycosylase"
FT REGION 415..709
FT /note="Transpeptidase"
FT ACT_SITE 200
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 476
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
SQ SEQUENCE 777 AA; 87324 MW; BCFC2676EA2AFF1C CRC64;
MTRKSSNRSR GRKARSGKSA SSSKLQIWLG RIWSIGWKLA LTLAAVLVFI GIYLDSMIKQ
RFEGQLFDLP TVVYARILTL EPGNGLSLQE LRNELDVLNY RKVAQPRFPG EYASSSSRIE
LIRRPFEFAD GPEPDRRVML TFDGSGLNKI ESLEQKRELG YLRLEPKLMG MLEKDSPEQR
LFLRRDQFPE VLVDALLVTE DRDFYQHDGV SPLAIGRAMV VNLKAGRTVQ GGSTLTQQLA
KNIFLSSDRT LWRKLREAYM ALIIDYRYSK DRILEAYLNE VYLGQSGADA IHGFGLASRL
YFGQPLQELR IDQLALLVGM VKGPSYYNPM RYAERARERR DLVLKLMMEH DILTAPEYQQ
AVTRPLDVQK TAQIASRQPA YFQQVSIELK EKLGDKFKAD SGLRVFTSLD PVSQSKLEQA
IHDQIPQLAK TAGKDLEAAA IAVDRHSGEI RAMVGGKRTG YDGFNRVLNA SRQIGSLVKP
AVYLTALAHP DQYNLATTLE DKPLTLKGSE GSAWTPRNYD RQYRGEVPLY LALAQSLNVP
TVALGMKLGI DQVSATLGKL GVNRDEIRPV PSMLLGSFSL TPYQVAQMYQ TLTNSGKKAP
LSALRSVLDL EGNVLYESLP RVSQAVDQQA AWLTTYAMKQ GVQEGTGRYL NAQFSSAALA
GKTGTTNDNR DSWFVGVDGR EVTTIWLGRD DNQPTKLTGA SGALRVYAQY LKYRIPEKLQ
LPWPEGITTF GFAKQTQGGL KLDCDNAFKL PIWDNQQQLK QQCENRPTEW IKKLFEW
