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Protein

Proline iminopeptidase

Gene

fpaP

Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Releases the N-terminal proline from various substrates. Cleaves specifically Pro-betaNA and small peptides containing proline at the amino terminal. No activity against hydroxyproline-betaNA.1 Publication

Catalytic activityi

Release of N-terminal proline from a peptide.1 Publication

pH dependencei

Optimum pH 8.0.1 Publication

Temperature dependencei

Maximum activity at 42 degrees Celsius. Stable at temperatures up to 44 degrees Celsius, showing 50% of activity after incubation at this temperature for 15 minutes (at pH 8.0).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei103 – 1031NucleophileBy similarity
Active sitei244 – 2441By similarity
Active sitei271 – 2711Proton donorBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Protein family/group databases

ESTHERiflame-pamp. Proline_iminopeptidase.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline iminopeptidaseBy similarity (EC:3.4.11.5)
Short name:
PIPBy similarity
Alternative name(s):
Prolyl aminopeptidase1 PublicationImported
Short name:
PAP1 Publication
Gene namesi
Name:fpaP
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298Proline iminopeptidasePRO_0000406320Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO05420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S33 family.Sequence analysis

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005945. Pro_imino_pep.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005539. Pept_S33_TRI_F1. 1 hit.
PRINTSiPR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01250. pro_imino_pep_2. 1 hit.

Sequencei

Sequence statusi: Complete.

O05420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPITTPVGN FKVWTKRFGT NPKIKVLLLH GGPAMTHEYM ECFETFFQRE
60 70 80 90 100
GFEFYEYDQL GSYYSDQPTD EKLWNIDRFV DEVEQVRKAI HADKENFYVL
110 120 130 140 150
GNSWGGILAM EYALKYQQNL KGLIVANMMA SAPEYVKYAE VLSKQMKPEV
160 170 180 190 200
LAEVRAIEAK KDYANPRYTE LLFPNYYAQH ICRLKEWPDA LNRSLKHVNS
210 220 230 240 250
TVYTLMQGPS ELGMSSDARL AKWDIKNRLH EIATPTLMIG ARYDTMDPKA
260 270 280 290
MEEQSKLVQK GRYLYCPNGS HLAMWDDQKV FMDGVIKFIK DVDTKSFN
Length:298
Mass (Da):34,613
Last modified:July 1, 1997 - v1
Checksum:iE5BA17298F949E69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83254 Genomic DNA. Translation: BAA19688.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83254 Genomic DNA. Translation: BAA19688.1.

3D structure databases

ProteinModelPortaliO05420.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiflame-pamp. Proline_iminopeptidase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005945. Pro_imino_pep.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005539. Pept_S33_TRI_F1. 1 hit.
PRINTSiPR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01250. pro_imino_pep_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPIP_ELIME
AccessioniPrimary (citable) accession number: O05420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: July 1, 1997
Last modified: September 16, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.