Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei233 – 2331Proton donor; for transglycosylase activityCurated
Active sitei510 – 5101Acyl-ester intermediate; for transpeptidase activity1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan biosynthetic process Source: EcoCyc
  • proteolysis Source: GOC
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10605. mrcB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6363CytoplasmicCuratedAdd
BLAST
Transmembranei64 – 8724Helical; Signal-anchor for type II membrane proteinCuratedAdd
BLAST
Topological domaini88 – 844757PeriplasmicCuratedAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi233 – 2331E → Q: Loss of wild-type glycan chain elongation activity. No complementation in strain defective in PBP-1b. 1 Publication
Mutagenesisi234 – 2341D → N: 7-fold decrease in catalytic activity. No complementation in strain defective in PBP-1b. 1 Publication
Mutagenesisi290 – 2901E → Q: 11-fold decrease in catalytic activity. Shows complementation activity in strain defective in PBP-1b. 1 Publication

Chemistry

ChEMBLiCHEMBL2354204.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 844844Penicillin-binding protein 1BPRO_0000012145Add
BLAST

Proteomic databases

EPDiP02919.
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 interactions.
DIPiDIP-10252N.
IntActiP02919. 9 interactions.
STRINGi511145.b0149.

Chemistry

BindingDBiP02919.

Structurei

Secondary structure

1
844
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni69 – 724Combined sources
Helixi76 – 8813Combined sources
Helixi90 – 934Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi111 – 1133Combined sources
Helixi121 – 13010Combined sources
Beta strandi144 – 1485Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi169 – 1768Combined sources
Beta strandi179 – 1857Combined sources
Turni186 – 1894Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi210 – 2123Combined sources
Helixi218 – 2203Combined sources
Helixi223 – 2319Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi237 – 2393Combined sources
Helixi241 – 2433Combined sources
Turni247 – 2493Combined sources
Helixi268 – 2769Combined sources
Beta strandi280 – 2823Combined sources
Helixi284 – 30017Combined sources
Helixi303 – 3108Combined sources
Turni311 – 3133Combined sources
Beta strandi314 – 3196Combined sources
Beta strandi322 – 3265Combined sources
Helixi327 – 3359Combined sources
Helixi339 – 3413Combined sources
Helixi344 – 35512Combined sources
Beta strandi356 – 3605Combined sources
Turni362 – 3643Combined sources
Helixi366 – 38217Combined sources
Helixi388 – 3958Combined sources
Beta strandi408 – 4114Combined sources
Helixi412 – 42615Combined sources
Turni429 – 4324Combined sources
Beta strandi433 – 4353Combined sources
Beta strandi437 – 4404Combined sources
Helixi444 – 46421Combined sources
Beta strandi471 – 4788Combined sources
Turni479 – 4813Combined sources
Beta strandi483 – 4886Combined sources
Beta strandi490 – 4923Combined sources
Helixi500 – 5034Combined sources
Helixi509 – 5124Combined sources
Helixi513 – 5219Combined sources
Turni524 – 5263Combined sources
Beta strandi532 – 5343Combined sources
Beta strandi543 – 5453Combined sources
Beta strandi561 – 5644Combined sources
Helixi565 – 5706Combined sources
Helixi574 – 58411Combined sources
Helixi586 – 59611Combined sources
Helixi600 – 6023Combined sources
Helixi607 – 6115Combined sources
Helixi618 – 62912Combined sources
Beta strandi632 – 6343Combined sources
Beta strandi640 – 6445Combined sources
Beta strandi646 – 6483Combined sources
Beta strandi650 – 6534Combined sources
Helixi664 – 67916Combined sources
Helixi684 – 6896Combined sources
Helixi691 – 6933Combined sources
Beta strandi696 – 7016Combined sources
Helixi703 – 7053Combined sources
Beta strandi706 – 7138Combined sources
Beta strandi715 – 72410Combined sources
Helixi737 – 74913Combined sources
Beta strandi763 – 7686Combined sources
Beta strandi774 – 7774Combined sources
Beta strandi780 – 7867Combined sources
Helixi792 – 7976Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FWLX-ray3.09A58-804[»]
3VMAX-ray2.16A58-804[»]
5FGZX-ray2.85A58-804[»]
ProteinModelPortaliP02919.
SMRiP02919. Positions 72-800.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02919.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 250163Membrane associationAdd
BLAST
Regioni109 – 20092UvrB domain 2 homologAdd
BLAST
Regioni195 – 367173TransglycosylaseAdd
BLAST
Regioni444 – 736293TranspeptidaseAdd
BLAST

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.
OMAiYRTIPVW.
OrthoDBiEOG6HMXCD.
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 CAA26099.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031P → A (PubMed:3882429).Curated
Sequence conflicti103 – 1031P → A (PubMed:8202364).Curated
Sequence conflicti754 – 7541P → PTP (PubMed:8202364).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545Missing in isoform Gamma. CuratedVSP_018737Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3FWLX-ray3.09A58-804[»]
3VMAX-ray2.16A58-804[»]
5FGZX-ray2.85A58-804[»]
ProteinModelPortaliP02919.
SMRiP02919. Positions 72-800.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP02919.
ChEMBLiCHEMBL2354204.
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

EPDiP02919.
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.
OMAiYRTIPVW.
OrthoDBiEOG6HMXCD.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12."
    Broome-Smith J.K., Edelman A., Yousif S., Spratt B.G.
    Eur. J. Biochem. 147:437-446(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 103 AND 754.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12."
    Keck W., Glauner B., Schwarz U., Broome-Smith J.K., Spratt B.G.
    Proc. Natl. Acad. Sci. U.S.A. 82:1999-2003(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 497-525.
    Strain: K12.
  6. "Localization of a putative second membrane association site in penicillin-binding protein 1B of Escherichia coli."
    Wang C.C., Schultz D.R., Nicholas R.A.
    Biochem. J. 316:149-156(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis."
    Lefevre F., Remy M.-H., Masson J.-M.
    J. Bacteriol. 179:4761-4767(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  8. "Use of a beta-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli."
    Edelman A., Bowler L., Broome-Smith J.K., Spratt B.G.
    Mol. Microbiol. 1:101-106(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  9. "Penicillin-binding protein 1B of Escherichia coli exists in dimeric forms."
    Zijderveld C.A., Aarsman M.E., den Blaauwen T., Nanninga N.
    J. Bacteriol. 173:5740-5746(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DIMERIZATION.
  10. "Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli."
    Vollmer W., von Rechenberg M., Hoeltje J.-V.
    J. Biol. Chem. 274:6726-6734(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIPA AND MLTA.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  11. "The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli."
    Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M., Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.
    Mol. Microbiol. 34:350-364(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE SER-510, MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
    Strain: EJ801.
  12. "Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs."
    Goffin C., Ghuysen J.-M.
    Microbiol. Mol. Biol. Rev. 62:1079-1093(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  13. "Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli."
    Sung M.-T., Lai Y.-T., Huang C.-Y., Chou L.-Y., Shih H.-W., Cheng W.-C., Wong C.-H., Ma C.
    Proc. Natl. Acad. Sci. U.S.A. 106:8824-8829(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 58-804 IN COMPLEX WITH MOENOMYCIN, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH MLTA; UVRA; FTSL AND FTSN, MEMBRANE TOPOLOGY, CATALYTIC ACTIVITY, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY.

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: May 11, 2016
This is version 180 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.