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Protein

Type 4 prepilin-like proteins leader peptide-processing enzyme

Gene

pilD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue. Processes the pilin precursor during membrane translocation. Required for the assembly of type IV pili and for secretion of most proteins.

Catalytic activityi

Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei72 – 721Important for activity
Sitei75 – 751Important for activity
Sitei97 – 971Important for activity
Sitei100 – 1001Important for activity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Methyltransferase, Protease, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi3.4.23.43. 5087.

Protein family/group databases

MEROPSiA24.001.
TCDBi3.A.15.2.1. the outer membrane protein secreting main terminal branch (mtb) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Type 4 prepilin-like proteins leader peptide-processing enzyme
Alternative name(s):
Protein PilD
Protein secretion protein XCPA
Including the following 2 domains:
Leader peptidase (EC:3.4.23.43)
Alternative name(s):
Prepilin peptidase
N-methyltransferase (EC:2.1.1.-)
Gene namesi
Name:pilD
Synonyms:xcpA
Ordered Locus Names:PA4528
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4528.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3321HelicalSequence analysisAdd
BLAST
Topological domaini34 – 12794CytoplasmicSequence analysisAdd
BLAST
Transmembranei128 – 14821HelicalSequence analysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Transmembranei183 – 20321HelicalSequence analysisAdd
BLAST
Transmembranei228 – 24821HelicalSequence analysisAdd
BLAST
Transmembranei261 – 27616HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Type 4 prepilin-like proteins leader peptide-processing enzymePRO_0000192625Add
BLAST

Proteomic databases

PaxDbiP22610.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA4528.

Structurei

3D structure databases

ProteinModelPortaliP22610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EHH. Bacteria.
COG1989. LUCA.
HOGENOMiHOG000248584.
InParanoidiP22610.
KOiK02654.
OMAiVFWLFKL.
OrthoDBiEOG6F55M8.
PhylomeDBiP22610.

Family and domain databases

InterProiIPR010627. Pept_A24A_N.
IPR014032. Peptidase_A24A_bac.
IPR000045. Prepilin_IV_endopep_pep.
[Graphical view]
PfamiPF06750. DiS_P_DiS. 1 hit.
PF01478. Peptidase_A24. 1 hit.
[Graphical view]
PRINTSiPR00864. PREPILNPTASE.

Sequencei

Sequence statusi: Complete.

P22610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLLDYLASH PLAFVLCTIL LGLLVGSFLN VVVHRLPKMM ERNWKAEARE
60 70 80 90 100
ALGLEPEPKQ ATYNLVLPNS ACPRCGHEIR PWENIPLVSY LALGGKCSSC
110 120 130 140 150
KAAIGKRYPL VELATALLSG YVAWHFGFTW QAGAMLLLTW GLLAMSLIDA
160 170 180 190 200
DHQLLPDVLV LPLLWLGLIA NHFGLFASLD DALFGAVFGY LSLWSVFWLF
210 220 230 240 250
KLVTGKEGMG YGDFKLLAML GAWGGWQILP LTILLSSLVG AILGVIMLRL
260 270 280 290
RNAESGTPIP FGPYLAIAGW IALLWGDQIT RTYLQFAGFK
Length:290
Mass (Da):31,870
Last modified:December 8, 2000 - v3
Checksum:i57A8526EB18FB752
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181T → A in strain: PAK.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32066 Genomic DNA. Translation: AAA25734.1.
M61096 Genomic DNA. Translation: AAA26023.1.
AE004091 Genomic DNA. Translation: AAG07916.1.
PIRiA39131.
RefSeqiNP_253218.1. NC_002516.2.
WP_003112839.1. NZ_ASJY01000735.1.

Genome annotation databases

EnsemblBacteriaiAAG07916; AAG07916; PA4528.
GeneIDi877861.
KEGGipae:PA4528.
PATRICi19843787. VBIPseAer58763_4739.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32066 Genomic DNA. Translation: AAA25734.1.
M61096 Genomic DNA. Translation: AAA26023.1.
AE004091 Genomic DNA. Translation: AAG07916.1.
PIRiA39131.
RefSeqiNP_253218.1. NC_002516.2.
WP_003112839.1. NZ_ASJY01000735.1.

3D structure databases

ProteinModelPortaliP22610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4528.

Protein family/group databases

MEROPSiA24.001.
TCDBi3.A.15.2.1. the outer membrane protein secreting main terminal branch (mtb) family.

Proteomic databases

PaxDbiP22610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07916; AAG07916; PA4528.
GeneIDi877861.
KEGGipae:PA4528.
PATRICi19843787. VBIPseAer58763_4739.

Organism-specific databases

PseudoCAPiPA4528.

Phylogenomic databases

eggNOGiENOG4105EHH. Bacteria.
COG1989. LUCA.
HOGENOMiHOG000248584.
InParanoidiP22610.
KOiK02654.
OMAiVFWLFKL.
OrthoDBiEOG6F55M8.
PhylomeDBiP22610.

Enzyme and pathway databases

BRENDAi3.4.23.43. 5087.

Family and domain databases

InterProiIPR010627. Pept_A24A_N.
IPR014032. Peptidase_A24A_bac.
IPR000045. Prepilin_IV_endopep_pep.
[Graphical view]
PfamiPF06750. DiS_P_DiS. 1 hit.
PF01478. Peptidase_A24. 1 hit.
[Graphical view]
PRINTSiPR00864. PREPILNPTASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Products of three accessory genes, pilB, pilC, and pilD, are required for biogenesis of Pseudomonas aeruginosa pili."
    Nunn D., Bergman S., Lory S.
    J. Bacteriol. 172:2911-2919(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: PAK.
  2. "Protein secretion in Pseudomonas aeruginosa: the xcpA gene encodes an integral inner membrane protein homologous to Klebsiella pneumoniae secretion function protein PulO."
    Bally M., Ball G., Badere A., Lazdunski A.
    J. Bacteriol. 173:479-486(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  4. "Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa -- a review."
    Lory S., Strom M.S.
    Gene 192:117-121(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "Posttranslational processing of type IV prepilin and homologs by PilD of Pseudomonas aeruginosa."
    Strom M.S., Nunn D.N., Lory S.
    Methods Enzymol. 235:527-540(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Identification of active-site cysteines in the conserved domain of PilD, the bifunctional type IV pilin leader peptidase/N-methyltransferase of Pseudomonas aeruginosa."
    Strom M.S., Bergman P., Lory S.
    J. Biol. Chem. 268:15788-15794(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYSTEINE RESIDUES.
  7. "Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa. Effect on leader peptidase and N-methyltransferase activities in vitro and in vivo."
    Pepe J.C., Lory S.
    J. Biol. Chem. 273:19120-19129(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-95 AND LYS-96.

Entry informationi

Entry nameiLEP4_PSEAE
AccessioniPrimary (citable) accession number: P22610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 8, 2000
Last modified: November 11, 2015
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.