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

Type 4 prepilin-like proteins leader peptide-processing enzyme

Gene

fimP

Organism
Dichelobacter nodosus (Bacteroides nodosus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue.By similarity

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.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Methyltransferase, Protease, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Protein family/group databases

MEROPSiA24.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Type 4 prepilin-like proteins leader peptide-processing enzyme
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:fimP
OrganismiDichelobacter nodosus (Bacteroides nodosus)
Taxonomic identifieri870 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalSequence analysisAdd
BLAST
Transmembranei106 – 12621HelicalSequence analysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Transmembranei161 – 18121HelicalSequence analysisAdd
BLAST
Transmembranei185 – 20521HelicalSequence analysisAdd
BLAST
Transmembranei231 – 25121HelicalSequence analysisAdd
BLAST
Transmembranei257 – 27721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Type 4 prepilin-like proteins leader peptide-processing enzymePRO_0000192617Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi246195.DNO_1124.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EHH. Bacteria.
COG1989. LUCA.

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.

Q46525-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLISELLQTP LGIFFVGLFS LMVGSFLNVV IYRVPVMMDR EEKQYAWQVF
60 70 80 90 100
HGEDSVCPEI PKQRFNLLVP ASRCPHCGHR IRAIENIPVI SWLFLKGKCS
110 120 130 140 150
GCGAAISARY LLVELLTAAL SVIVAFHYHD PLSLGFALVF TWTLIALCFI
160 170 180 190 200
DAEHQLLPDR LTLPLLWLGI LAALFNVFIN LESSVIGAMI GYLSLWSVYW
210 220 230 240 250
LFKLITGREG MGYGDFKLLA CLCAWQGAWM LPIILFSAAI LGMIYALGIG
260 270 280
LRMGKPMPFG PFLAIAGWLT FLYGAQIGQL FGYFPA
Length:286
Mass (Da):31,863
Last modified:November 1, 1996 - v1
Checksum:i6EF18DA03FC175DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17138 Genomic DNA. Translation: AAB65807.1.
RefSeqiWP_012031428.1. NZ_LGVW01000028.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17138 Genomic DNA. Translation: AAB65807.1.
RefSeqiWP_012031428.1. NZ_LGVW01000028.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246195.DNO_1124.

Protein family/group databases

MEROPSiA24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105EHH. Bacteria.
COG1989. LUCA.

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

  1. "Identification of fimbrial assembly genes from Dichelobacter nodosus: evidence that fimP encodes the type-IV prepilin peptidase."
    Johnston J.L., Billington S.J., Haring V., Rood J.I.
    Gene 161:21-26(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A198.

Entry informationi

Entry nameiLEP4_DICNO
AccessioniPrimary (citable) accession number: Q46525
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 11, 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

Keywords - Technical termi

Multifunctional enzyme

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.