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UniProtKB - P02919 (PBPB_ECOLI)

Protein

Penicillin-binding protein 1B

Gene

mrcB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).

Miscellaneous

A third isozyme, Beta, lacking the first 25 N-terminal amino acids of the isoform Alpha and a fourth isozyme, Delta, have been found, but seem to result from the artifactual degradation of the isoform Alpha and isoform Gamma respectively.

Catalytic activityi

(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate.2 Publications
Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.1 Publication

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei233Proton donor; for transglycosylase activity1 Publication1
Active sitei510Acyl-ester intermediate; for transpeptidase activity1 Publication1

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan biosynthetic process Source: EcoCyc
  • regulation of cell shape Source: EcoCyc
  • response to antibiotic Source: EcoCyc
  • response to X-ray Source: EcoCyc
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionCarboxypeptidase, Glycosyltransferase, Hydrolase, Multifunctional enzyme, Protease, Transferase
Biological processAntibiotic resistance, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG10605-MONOMER
MetaCyc:EG10605-MONOMER
BRENDAi2.4.1.129 2026
UniPathwayi
UPA00219

Protein family/group databases

CAZyiGT51 Glycosyltransferase Family 51

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin-binding protein 1B
Short name:
PBP-1b
Short name:
PBP1b
Alternative name(s):
Murein polymerase
Including the following 2 domains:
Penicillin-insensitive transglycosylase (EC:2.4.1.1292 Publications)
Alternative name(s):
Peptidoglycan TGase
Peptidoglycan glycosyltransferase
Penicillin-sensitive transpeptidase (EC:3.4.16.41 Publication)
Alternative name(s):
DD-transpeptidase
Gene namesi
Name:mrcB
Synonyms:pbpF, ponB
Ordered Locus Names:b0149, JW0145
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10605 mrcB

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 63CytoplasmicCuratedAdd BLAST63
Transmembranei64 – 87Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST24
Topological domaini88 – 844PeriplasmicCuratedAdd BLAST757

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi233E → Q: Loss of wild-type glycan chain elongation activity. No complementation in strain defective in PBP-1b. 1 Publication1
Mutagenesisi234D → N: 7-fold decrease in catalytic activity. No complementation in strain defective in PBP-1b. 1 Publication1
Mutagenesisi290E → Q: 11-fold decrease in catalytic activity. Shows complementation activity in strain defective in PBP-1b. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1814
DrugBankiDB01414 Cefacetrile
DB01327 Cefazolin
DB00274 Cefmetazole
DB01328 Cefonicid
DB01329 Cefoperazone
DB01331 Cefoxitin
DB00430 Cefpiramide
DB00438 Ceftazidime
DB01415 Ceftibuten
DB01332 Ceftizoxime
DB06211 Doripenem
DB00303 Ertapenem
DB01598 Imipenem
DB04570 Latamoxef

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000121451 – 844Penicillin-binding protein 1BAdd BLAST844

Proteomic databases

PaxDbiP02919
PRIDEiP02919

Interactioni

Subunit structurei

Forms a trimeric complex with MipA and MltA. Has also been shown to exist as monomer or homodimer; homodimer of Alpha and Gamma isozymes can be found. Interacts with UvrA, FtsL and FtsN.2 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi4260880, 259 interactors
DIPiDIP-10252N
IntActiP02919, 15 interactors
STRINGi316385.ECDH10B_0129

Chemistry databases

BindingDBiP02919

Structurei

Secondary structure

1844
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP02919
SMRiP02919
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02919

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni88 – 250Membrane associationAdd BLAST163
Regioni109 – 200UvrB domain 2 homologAdd BLAST92
Regioni195 – 367TransglycosylaseAdd BLAST173
Regioni444 – 736TranspeptidaseAdd BLAST293

Domaini

The UvrB domain 2 homolog region (UB2H domain) is important for interaction with MltA.1 Publication

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyltransferase 51 family.Curated
In the C-terminal section; belongs to the transpeptidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZ4 Bacteria
COG0744 LUCA
HOGENOMiHOG000282711
InParanoidiP02919
KOiK05365
OMAiVHGMGLA
PhylomeDBiP02919

Family and domain databases

Gene3Di1.10.3810.10, 2 hits
InterProiView protein in InterPro
IPR012338 Beta-lactam/transpept-like
IPR001264 Glyco_trans_51
IPR023346 Lysozyme-like_dom_sf
IPR032730 PBP1b_TM
IPR011813 PBP_1b
IPR036950 PBP_transglycosylase
IPR001460 PCN-bd_Tpept
IPR028166 UB2H
PfamiView protein in Pfam
PF14812 PBP1_TM, 1 hit
PF00912 Transgly, 1 hit
PF00905 Transpeptidase, 1 hit
PF14814 UB2H, 1 hit
PIRSFiPIRSF002799 PBP_1b, 1 hit
SUPFAMiSSF53955 SSF53955, 1 hit
SSF56601 SSF56601, 2 hits
TIGRFAMsiTIGR02071 PBP_1b, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket
Isoform Alpha (identifier: P02919-1) [UniParc]FASTAAdd to basket
Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG 
        60         70         80         90        100
KGKGKGRKPR GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW 
       110        120        130        140        150
QLPAAVYGRM VNLEPDMTIS KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN 
       160        170        180        190        200
SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL ATIVNMENNR QFGFFRLDPR 
       210        220        230        240        250
LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH DGISLYSIGR 
       260        270        280        290        300
AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR 
       310        320        330        340        350
YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL 
       360        370        380        390        400
VGMVKGASIY NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG 
       410        420        430        440        450
VQPRGGVISP QPAFMQLVRQ ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA 
       460        470        480        490        500
EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF SGEVRAMVGG SEPQFAGYNR 
       510        520        530        540        550
AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL RQPNGQVWSP 
       560        570        580        590        600
QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK 
       610        620        630        640        650
DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV 
       660        670        680        690        700
LYQSFPQAER AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG 
       710        720        730        740        750
TTNNNVDTWF AGIDGSTVTI TWVGRDNNQP TKLYGASGAM SIYQRYLANQ 
       760        770        780        790        800
TPTPLNLVPP EDIADMGVDY DGNFVCSGGM RILPVWTSDP QSLCQQSEMQ 
       810        820        830        840 
QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM FGSN
Length:844
Mass (Da):94,293
Last modified:July 19, 2003 - v2
Checksum:iCED0A19FAC73961E
GO
Isoform Gamma (identifier: P02919-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.

Show »
Length:799
Mass (Da):88,890
Checksum:i2A4869BED79A2530
GO

Sequence cautioni

The sequence CAA26099 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103P → A (PubMed:3882429).Curated1
Sequence conflicti103P → A (PubMed:8202364).Curated1
Sequence conflicti754P → PTP (PubMed:8202364).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0187371 – 45Missing in isoform Gamma. CuratedAdd BLAST45

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02163 Genomic DNA Translation: CAA26098.1
X02163 Genomic DNA Translation: CAA26099.1 Different initiation.
U00096 Genomic DNA Translation: AAC73260.1
AP009048 Genomic DNA Translation: BAB96725.2
PIRiE64738 ZPECPB
RefSeqiNP_414691.1, NC_000913.3
WP_000918162.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73260; AAC73260; b0149
BAB96725; BAB96725; BAB96725
GeneIDi944843
KEGGiecj:JW0145
eco:b0149
PATRICifig|1411691.4.peg.2132

Keywords - Coding sequence diversityi

Alternative initiation

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02163 Genomic DNA Translation: CAA26098.1
X02163 Genomic DNA Translation: CAA26099.1 Different initiation.
U00096 Genomic DNA Translation: AAC73260.1
AP009048 Genomic DNA Translation: BAB96725.2
PIRiE64738 ZPECPB
RefSeqiNP_414691.1, NC_000913.3
WP_000918162.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FWLX-ray3.09A58-804[»]
3VMAX-ray2.16A58-804[»]
5FGZX-ray2.85A58-804[»]
5HL9X-ray2.70A58-804[»]
5HLAX-ray2.36A58-804[»]
5HLBX-ray2.42A58-804[»]
5HLDX-ray2.31A58-804[»]
ProteinModelPortaliP02919
SMRiP02919
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260880, 259 interactors
DIPiDIP-10252N
IntActiP02919, 15 interactors
STRINGi316385.ECDH10B_0129

Chemistry databases

BindingDBiP02919
ChEMBLiCHEMBL1814
DrugBankiDB01414 Cefacetrile
DB01327 Cefazolin
DB00274 Cefmetazole
DB01328 Cefonicid
DB01329 Cefoperazone
DB01331 Cefoxitin
DB00430 Cefpiramide
DB00438 Ceftazidime
DB01415 Ceftibuten
DB01332 Ceftizoxime
DB06211 Doripenem
DB00303 Ertapenem
DB01598 Imipenem
DB04570 Latamoxef

Protein family/group databases

CAZyiGT51 Glycosyltransferase Family 51

Proteomic databases

PaxDbiP02919
PRIDEiP02919

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73260; AAC73260; b0149
BAB96725; BAB96725; BAB96725
GeneIDi944843
KEGGiecj:JW0145
eco:b0149
PATRICifig|1411691.4.peg.2132

Organism-specific databases

EchoBASEiEB0600
EcoGeneiEG10605 mrcB

Phylogenomic databases

eggNOGiENOG4105BZ4 Bacteria
COG0744 LUCA
HOGENOMiHOG000282711
InParanoidiP02919
KOiK05365
OMAiVHGMGLA
PhylomeDBiP02919

Enzyme and pathway databases

UniPathwayi
UPA00219

BioCyciEcoCyc:EG10605-MONOMER
MetaCyc:EG10605-MONOMER
BRENDAi2.4.1.129 2026

Miscellaneous databases

EvolutionaryTraceiP02919
PROiPR:P02919

Family and domain databases

Gene3Di1.10.3810.10, 2 hits
InterProiView protein in InterPro
IPR012338 Beta-lactam/transpept-like
IPR001264 Glyco_trans_51
IPR023346 Lysozyme-like_dom_sf
IPR032730 PBP1b_TM
IPR011813 PBP_1b
IPR036950 PBP_transglycosylase
IPR001460 PCN-bd_Tpept
IPR028166 UB2H
PfamiView protein in Pfam
PF14812 PBP1_TM, 1 hit
PF00912 Transgly, 1 hit
PF00905 Transpeptidase, 1 hit
PF14814 UB2H, 1 hit
PIRSFiPIRSF002799 PBP_1b, 1 hit
SUPFAMiSSF53955 SSF53955, 1 hit
SSF56601 SSF56601, 2 hits
TIGRFAMsiTIGR02071 PBP_1b, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPBPB_ECOLI
AccessioniPrimary (citable) accession number: P02919
Secondary accession number(s): P75664
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2003
Last modified: March 28, 2018
This is version 194 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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