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

Beta-lactam-inducible penicillin-binding protein

Gene

pbp

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251PenicillinCurated
Binding sitei405 – 4051PenicillinCurated

GO - Molecular functioni

  1. penicillin binding Source: InterPro

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. cell wall organization Source: UniProtKB-KW
  4. peptidoglycan biosynthetic process Source: UniProtKB-KW
  5. regulation of cell shape Source: UniProtKB-KW
  6. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactam-inducible penicillin-binding protein
Gene namesi
Name:pbp
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2421HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 670670Beta-lactam-inducible penicillin-binding proteinPRO_0000195443Add
BLAST

Expressioni

Inductioni

In the presence of beta-lactam antibiotics, MRSA cells produce this unique PBP in excessively large amounts and can still proliferate, while all the normal PBPs are inactivated (reversible switching ability of PBP formation).

Structurei

3D structure databases

SMRiP07944. Positions 27-670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transpeptidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0768.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR007887. MecA_N.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF05223. MecA_N. 1 hit.
PF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.

Sequencei

Sequence statusi: Complete.

P07944-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIKIVPLI LIVVVVGFGI YFYASKDKEI NNTIDAIEDK NFKQVYKDSS
60 70 80 90 100
YISKSDNGEV EMTERPIKIY NSLGVKDINI QDRKIKKVSK NKKRVDAQYK
110 120 130 140 150
IKTNYGNIDR NVQFNFVKED GMWKLDWDHS VIIPGMQKDQ SIHIENLKSE
160 170 180 190 200
RGKILDRNNV ELANTGTHMR LGIVPKNVSK KDYKAIAKEL SISEDYINNK
210 220 230 240 250
WIKIGYKMIP SFHFKTVKKM DEYLSDFAKK FHLTTNETES RNYPLGKATS
260 270 280 290 300
HLLGYVGPIN SEELKQKEYK GYKDDAVIGK KGLEKLYDKK LQHEDGYRVT
310 320 330 340 350
IVRVDDNSNT IAHTLIEKKK KDGKDIQLTI DAKVQKSIYN NMKNDYGSGT
360 370 380 390 400
AIHPQTGELL ALVSTPSYDV YPFMYGMSNE EYNKLTEDKK EPLLNKFQIT
410 420 430 440 450
TSPGSTQKIL TAMIGLNNKT LDDKTSYKID GKGWQKDKSW GGYNVTRYEV
460 470 480 490 500
VNGNIDLKQA IESSDNIFFA RVALELGSKK FEKGMKKLGV GEDIPSDYPF
510 520 530 540 550
YNAQISNKNL DNEILLADSG YGQGEILINP VQILSIYSAL ENNGNINAPH
560 570 580 590 600
LLKDTKNKVW KKNIISKENI NLLNDGMQQV VNKTHKEDIY RSYANLIGKS
610 620 630 640 650
GTAELKMKQG ETGRQIGWFI SYDKDNPNMM MAINVKDVQD KGMASYNAKI
660 670
SGKVYDELYE NGNKKYDIDE
Length:670
Mass (Da):76,463
Last modified:August 1, 1988 - v1
Checksum:i2DAA414D35DA993A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00688 Genomic DNA. Translation: CAA68684.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00688 Genomic DNA. Translation: CAA68684.1.

3D structure databases

SMRiP07944. Positions 27-670.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0768.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR007887. MecA_N.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamiPF05223. MecA_N. 1 hit.
PF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMiSSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Evolution of an inducible penicillin-target protein in methicillin-resistant Staphylococcus aureus by gene fusion."
    Song M.D., Wachi M., Doi M., Ishino F., Matsuhashi M.
    FEBS Lett. 221:167-171(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPBP_STAAU
AccessioniPrimary (citable) accession number: P07944
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 1, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

PBP has extremely low affinity to penicillin and most other beta-lactam antibiotics.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.