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P32722 (PORD_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Porin D

EC=3.4.21.-
Alternative name(s):
Imipenem/basic amino acid-specific outer membrane pore
Outer membrane protein D2
Gene names
Name:oprD
Ordered Locus Names:PA0958
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Porin with a specificity for basic amino acids. Also possesses serine protease activity. Ref.5 Ref.6

Subcellular location

Cell outer membrane; Multi-pass membrane protein Ref.5.

Sequence similarities

Belongs to the outer membrane porin (Opr) (TC 1.B.25) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.2 Ref.4
Chain24 – 443420Porin D
PRO_0000027336

Sites

Active site1791 Ref.7
Active site2311 Ref.7
Active site3191 Ref.7

Experimental info

Mutagenesis1791H → Q: Loss of protease activity. No effect on porin activity. Ref.7
Mutagenesis2311D → N: Loss of protease activity. No effect on porin activity. Ref.7
Mutagenesis3191S → A: Loss of protease activity. No effect on porin activity. Ref.7
Mutagenesis3901H → Q: No effect on protease activity. Ref.7
Sequence conflict441L → Y AA sequence Ref.2

Secondary structure

....................................................... 443
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32722 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: E083FFE074DCFB64

FASTA44348,360
        10         20         30         40         50         60 
MKVMKWSAIA LAVSAGSTQF AVADAFVSDQ AEAKGFIEDS SLDLLLRNYY FNRDGKSGSG 

        70         80         90        100        110        120 
DRVDWTQGFL TTYESGFTQG TVGFGVDAFG YLGLKLDGTS DKTGTGNLPV MNDGKPRDDY 

       130        140        150        160        170        180 
SRAGGAVKVR ISKTMLKWGE MQPTAPVFAA GGSRLFPQTA TGFQLQSSEF EGLDLEAGHF 

       190        200        210        220        230        240 
TEGKEPTTVK SRGELYATYA GETAKSADFI GGRYAITDNL SASLYGAELE DIYRQYYLNS 

       250        260        270        280        290        300 
NYTIPLASDQ SLGFDFNIYR TNDEGKAKAG DISNTTWSLA AAYTLDAHTF TLAYQKVHGD 

       310        320        330        340        350        360 
QPFDYIGFGR NGSGAGGDSI FLANSVQYSD FNGPGEKSWQ ARYDLNLASY GVPGLTFMVR 

       370        380        390        400        410        420 
YINGKDIDGT KMSDNNVGYK NYGYGEDGKH HETNLEAKYV VQSGPAKDLS FRIRQAWHRA 

       430        440 
NADQGEGDQN EFRLIVDYPL SIL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the protein D2 gene of Pseudomonas aeruginosa."
Yoneyama H., Yoshihara E., Nakae T.
Antimicrob. Agents Chemother. 36:1791-1793(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of two gene regions involved in the expression of the imipenem-specific, outer membrane porin protein OprD of Pseudomonas aeruginosa."
Huang H., Siehnel R.J., Bellido F., Rawling E., Hancock R.E.W.
FEMS Microbiol. Lett. 76:267-274(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-40.
Strain: ATCC 15692 / PAO1 / H103.
[3]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[4]"Two-dimensional polyacrylamide gel electrophoresis isolation and microsequencing of Pseudomonas aeruginosa proteins."
Michea-Hamzehpour M., Sanchez J.-C., Epp S.F., Paquet N., Hughes G.J., Hochstrasser D.F., Pechere J.-C.
Enzyme Protein 47:1-8(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-48.
[5]"Protein D2 channel of the Pseudomonas aeruginosa outer membrane has a binding site for basic amino acids and peptides."
Trias J., Nikaido H.
J. Biol. Chem. 265:15680-15684(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the protease activity."
Yoshihara E., Gotoh N., Nishino T., Nakae T.
FEBS Lett. 394:179-182(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A SERINE PROTEASE.
[7]"Identification of the catalytic triad of the protein D2 protease in Pseudomonas aeruginosa."
Yoshihara E., Yoneyama H., Ono T., Nakae T.
Biochem. Biophys. Res. Commun. 247:142-145(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-179; ASP-231; SER-319 AND HIS-390, ACTIVE SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63152 Genomic DNA. Translation: CAA44855.1.
Z14065 Genomic DNA. Translation: CAA78448.1.
AE004091 Genomic DNA. Translation: AAG04347.1.
PIRS23771.
RefSeqNP_249649.1. NC_002516.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ODJX-ray2.90A/B26-443[»]
3SY7X-ray2.15A24-443[»]
4FOZX-ray2.40A24-443[»]
ProteinModelPortalP32722.
SMRP32722. Positions 24-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29627N.
STRING208964.PA0958.

Protein family/group databases

TCDB1.B.25.1.1. the outer membrane porin (opr) family.

Proteomic databases

PRIDEP32722.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG04347; AAG04347; PA0958.
GeneID881970.
KEGGpae:PA0958.
PATRIC19836216. VBIPseAer58763_0996.

Organism-specific databases

PseudoCAPPA0958.

Phylogenomic databases

eggNOGNOG14525.
HOGENOMHOG000220145.
KOK18093.
OMAHTFTLAY.
OrthoDBEOG63Z742.
PhylomeDBP32722.

Family and domain databases

Gene3D2.40.160.10. 1 hit.
InterProIPR005318. OM_porin_bac.
IPR023614. Porin_dom.
[Graphical view]
PfamPF03573. OprD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32722.

Entry information

Entry namePORD_PSEAE
AccessionPrimary (citable) accession number: P32722
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references