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Protein

Penicillin-binding protein 1B

Gene

mrcB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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).

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.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 activityCurated1
Active sitei510Acyl-ester intermediate; for transpeptidase activity1 Publication1

GO - Molecular functioni

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
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Hydrolase, Transferase

Keywords - Biological processi

Antibiotic resistance, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG10605-MONOMER.
ECOL316407:JW0145-MONOMER.
MetaCyc:EG10605-MONOMER.
BRENDAi2.4.1.129. 2026.
UniPathwayiUPA00219.

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:2.4.1.129)
Alternative name(s):
Peptidoglycan TGase
Peptidoglycan glycosyltransferase
Penicillin-sensitive transpeptidase (EC:3.4.-.-)
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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

  • integral component of external side of plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
  • peptidoglycan-based cell wall Source: InterPro
  • plasma membrane Source: EcoCyc
Complete GO annotation...

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

WithEntry#Exp.IntActNotes
ftsNP291316EBI-909769,EBI-1134233
lpoBP0AB384EBI-909769,EBI-3405489

Protein-protein interaction databases

BioGridi4260880. 237 interactors.
DIPiDIP-10252N.
IntActiP02919. 9 interactors.
STRINGi511145.b0149.

Chemistry databases

BindingDBiP02919.

Structurei

Secondary structure

1844
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni69 – 72Combined sources4
Helixi76 – 88Combined sources13
Helixi90 – 93Combined sources4
Beta strandi104 – 107Combined sources4
Beta strandi111 – 113Combined sources3
Helixi121 – 130Combined sources10
Beta strandi144 – 148Combined sources5
Beta strandi151 – 156Combined sources6
Beta strandi159 – 161Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi169 – 176Combined sources8
Beta strandi179 – 185Combined sources7
Turni186 – 189Combined sources4
Beta strandi193 – 196Combined sources4
Beta strandi201 – 205Combined sources5
Beta strandi210 – 212Combined sources3
Helixi218 – 220Combined sources3
Helixi223 – 231Combined sources9
Beta strandi234 – 236Combined sources3
Beta strandi237 – 239Combined sources3
Helixi241 – 243Combined sources3
Turni247 – 249Combined sources3
Helixi268 – 276Combined sources9
Beta strandi280 – 282Combined sources3
Helixi284 – 300Combined sources17
Helixi303 – 310Combined sources8
Turni311 – 313Combined sources3
Beta strandi314 – 319Combined sources6
Beta strandi322 – 326Combined sources5
Helixi327 – 335Combined sources9
Helixi339 – 341Combined sources3
Helixi344 – 355Combined sources12
Beta strandi356 – 360Combined sources5
Turni362 – 364Combined sources3
Helixi366 – 382Combined sources17
Helixi388 – 395Combined sources8
Beta strandi408 – 411Combined sources4
Helixi412 – 426Combined sources15
Turni429 – 432Combined sources4
Beta strandi433 – 435Combined sources3
Beta strandi437 – 440Combined sources4
Helixi444 – 464Combined sources21
Beta strandi471 – 478Combined sources8
Turni479 – 481Combined sources3
Beta strandi483 – 488Combined sources6
Beta strandi490 – 492Combined sources3
Helixi500 – 503Combined sources4
Helixi509 – 512Combined sources4
Helixi513 – 521Combined sources9
Turni524 – 526Combined sources3
Beta strandi532 – 534Combined sources3
Beta strandi543 – 545Combined sources3
Beta strandi561 – 564Combined sources4
Helixi565 – 570Combined sources6
Helixi574 – 584Combined sources11
Helixi586 – 596Combined sources11
Helixi600 – 602Combined sources3
Helixi607 – 611Combined sources5
Helixi618 – 629Combined sources12
Beta strandi632 – 634Combined sources3
Beta strandi640 – 644Combined sources5
Beta strandi646 – 648Combined sources3
Beta strandi650 – 653Combined sources4
Helixi664 – 679Combined sources16
Helixi684 – 689Combined sources6
Helixi691 – 693Combined sources3
Beta strandi696 – 701Combined sources6
Helixi703 – 705Combined sources3
Beta strandi706 – 713Combined sources8
Beta strandi715 – 724Combined sources10
Helixi737 – 749Combined sources13
Beta strandi763 – 768Combined sources6
Beta strandi774 – 777Combined sources4
Beta strandi780 – 786Combined sources7
Helixi792 – 797Combined sources6

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[»]
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.
OMAiRALMANY.
PhylomeDBiP02919.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR001264. Glyco_trans_51.
IPR023346. Lysozyme-like_dom.
IPR032730. PBP1b_TM.
IPR011813. PBP_1b.
IPR001460. PCN-bd_Tpept.
IPR028166. UB2H.
[Graphical view]
PfamiPF14812. PBP1_TM. 1 hit.
PF00912. Transgly. 1 hit.
PF00905. Transpeptidase. 1 hit.
PF14814. UB2H. 1 hit.
[Graphical view]
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.
PATRICi32115405. VBIEscCol129921_0154.

Keywords - Coding sequence diversityi

Alternative initiation

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[»]
ProteinModelPortaliP02919.
SMRiP02919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260880. 237 interactors.
DIPiDIP-10252N.
IntActiP02919. 9 interactors.
STRINGi511145.b0149.

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.
PATRICi32115405. VBIEscCol129921_0154.

Organism-specific databases

EchoBASEiEB0600.
EcoGeneiEG10605. mrcB.

Phylogenomic databases

eggNOGiENOG4105BZ4. Bacteria.
COG0744. LUCA.
HOGENOMiHOG000282711.
InParanoidiP02919.
KOiK05365.
OMAiRALMANY.
PhylomeDBiP02919.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciEcoCyc:EG10605-MONOMER.
ECOL316407:JW0145-MONOMER.
MetaCyc:EG10605-MONOMER.
BRENDAi2.4.1.129. 2026.

Miscellaneous databases

EvolutionaryTraceiP02919.
PROiP02919.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR001264. Glyco_trans_51.
IPR023346. Lysozyme-like_dom.
IPR032730. PBP1b_TM.
IPR011813. PBP_1b.
IPR001460. PCN-bd_Tpept.
IPR028166. UB2H.
[Graphical view]
PfamiPF14812. PBP1_TM. 1 hit.
PF00912. Transgly. 1 hit.
PF00905. Transpeptidase. 1 hit.
PF14814. UB2H. 1 hit.
[Graphical view]
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 historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2003
Last modified: November 2, 2016
This is version 184 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.