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P07944

- PBP_STAAU

UniProt

P07944 - PBP_STAAU

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Protein

Beta-lactam-inducible penicillin-binding protein

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

Functioni

Sites

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

GO - Molecular functioni

  1. penicillin binding Source: InterPro

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. peptidoglycan biosynthetic process Source: UniProtKB-KW
  4. regulation of cell shape Source: UniProtKB-KW
  5. 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 – 2421Helical; Reviewed predictionAdd
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

ProteinModelPortaliP07944.
SMRiP07944. Positions 27-670.

Family & Domainsi

Sequence similaritiesi

Belongs to the transpeptidase family.

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

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MKKIKIVPLI LIVVVVGFGI YFYASKDKEI NNTIDAIEDK NFKQVYKDSS    50
YISKSDNGEV EMTERPIKIY NSLGVKDINI QDRKIKKVSK NKKRVDAQYK 100
IKTNYGNIDR NVQFNFVKED GMWKLDWDHS VIIPGMQKDQ SIHIENLKSE 150
RGKILDRNNV ELANTGTHMR LGIVPKNVSK KDYKAIAKEL SISEDYINNK 200
WIKIGYKMIP SFHFKTVKKM DEYLSDFAKK FHLTTNETES RNYPLGKATS 250
HLLGYVGPIN SEELKQKEYK GYKDDAVIGK KGLEKLYDKK LQHEDGYRVT 300
IVRVDDNSNT IAHTLIEKKK KDGKDIQLTI DAKVQKSIYN NMKNDYGSGT 350
AIHPQTGELL ALVSTPSYDV YPFMYGMSNE EYNKLTEDKK EPLLNKFQIT 400
TSPGSTQKIL TAMIGLNNKT LDDKTSYKID GKGWQKDKSW GGYNVTRYEV 450
VNGNIDLKQA IESSDNIFFA RVALELGSKK FEKGMKKLGV GEDIPSDYPF 500
YNAQISNKNL DNEILLADSG YGQGEILINP VQILSIYSAL ENNGNINAPH 550
LLKDTKNKVW KKNIISKENI NLLNDGMQQV VNKTHKEDIY RSYANLIGKS 600
GTAELKMKQG ETGRQIGWFI SYDKDNPNMM MAINVKDVQD KGMASYNAKI 650
SGKVYDELYE NGNKKYDIDE 670
Length:670
Mass (Da):76,463
Last modified:August 1, 1988 - v1
Checksum:i2DAA414D35DA993A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00688 Genomic DNA. Translation: CAA68684.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00688 Genomic DNA. Translation: CAA68684.1 .

3D structure databases

ProteinModelPortali P07944.
SMRi P07944. Positions 27-670.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0768.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
InterProi IPR012338. Beta-lactam/transpept-like.
IPR007887. MecA_N.
IPR005311. PBP_dimer.
IPR001460. PCN-bd_Tpept.
[Graphical view ]
Pfami PF05223. MecA_N. 1 hit.
PF03717. PBP_dimer. 1 hit.
PF00905. Transpeptidase. 1 hit.
[Graphical view ]
SUPFAMi SSF56519. SSF56519. 1 hit.
SSF56601. SSF56601. 1 hit.
ProtoNeti Search...

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(1987) [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: February 19, 2014
This is version 71 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

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