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Protein

Proline iminopeptidase

Gene

pip

Organism
Xanthomonas citri (Xanthomonas campestris pv. citri)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in proline metabolism and sensitivity to ascamycin. Has ascamycin dealanylating activity.

Catalytic activityi

Release of N-terminal proline from a peptide.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei110Nucleophile1 Publication1
Active sitei2661 Publication1
Active sitei294Proton donor1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Protein family/group databases

ESTHERixanca-impep. Proline_iminopeptidase.
MEROPSiS33.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline iminopeptidase (EC:3.4.11.5)
Short name:
PIP
Alternative name(s):
Prolyl aminopeptidase
Short name:
PAP
Gene namesi
Name:pip
Synonyms:xap
OrganismiXanthomonas citri (Xanthomonas campestris pv. citri)
Taxonomic identifieri346 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000808471 – 313Proline iminopeptidaseAdd BLAST313

Interactioni

Subunit structurei

Homooligomer.

Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 17Combined sources7
Beta strandi19 – 21Combined sources3
Beta strandi23 – 30Combined sources8
Beta strandi34 – 40Combined sources7
Turni43 – 46Combined sources4
Helixi50 – 55Combined sources6
Turni58 – 60Combined sources3
Beta strandi61 – 66Combined sources6
Beta strandi74 – 76Combined sources3
Helixi85 – 98Combined sources14
Beta strandi102 – 109Combined sources8
Helixi111 – 122Combined sources12
Helixi124 – 126Combined sources3
Beta strandi127 – 134Combined sources8
Helixi140 – 147Combined sources8
Helixi151 – 154Combined sources4
Helixi156 – 164Combined sources9
Helixi168 – 170Combined sources3
Helixi174 – 182Combined sources9
Helixi187 – 203Combined sources17
Beta strandi205 – 208Combined sources4
Helixi211 – 217Combined sources7
Helixi220 – 235Combined sources16
Helixi237 – 239Combined sources3
Helixi245 – 248Combined sources4
Helixi250 – 253Combined sources4
Beta strandi258 – 263Combined sources6
Beta strandi267 – 269Combined sources3
Helixi271 – 280Combined sources10
Beta strandi284 – 289Combined sources6
Helixi299 – 312Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZWX-ray2.70A/B1-313[»]
ProteinModelPortaliP52279.
SMRiP52279.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52279.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 298AB hydrolase-1Sequence analysisAdd BLAST264

Sequence similaritiesi

Belongs to the peptidase S33 family.Curated

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005944. Pro_iminopeptidase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006431. Pept_S33. 1 hit.
PRINTSiPR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01249. pro_imino_pep_1. 1 hit.

Sequencei

Sequence statusi: Complete.

P52279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLYPEITP YQQGSLKVDD RHTLYFEQCG NPHGKPVVML HGGPGGGCND
60 70 80 90 100
KMRRFHDPAK YRIVLFDQRG SGRSTPHADL VDNTTWDLVA DIERLRTHLG
110 120 130 140 150
VDRWQVFGGS WGSTLALAYA ADPSAAGHQL VLRGIFLLRR FELEWFYQEG
160 170 180 190 200
ASRLFPDAWE HYLNAIPPVE RADLMSAFHR RLTSDDEATR LAAAKAWSVW
210 220 230 240 250
EGATSFLHVD EDFVTGHEDA HFALAFARIE NHYFVNGGFF EVEDQLLRDA
260 270 280 290 300
HRIADIPGVI VHGRYDVVCP LQSAWDLHKA WPKAQLQISP ASGHSAFEPE
310
NVDALVRATD GFA
Length:313
Mass (Da):35,260
Last modified:November 1, 1997 - v2
Checksum:i7A9DF2636363FF48
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti95L → V in BAA11623 (PubMed:8870654).Curated1
Sequence conflicti121 – 129ADPSAAGHQ → QTHPQQVTE in BAA11623 (PubMed:8870654).Curated9
Sequence conflicti245 – 251QLLRDAH → SCCATD in BAA11623 (PubMed:8870654).Curated7
Sequence conflicti284Missing in BAA11623 (PubMed:8870654).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54150 Genomic DNA. Translation: CAA90864.1.
D82882 Genomic DNA. Translation: BAA11623.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54150 Genomic DNA. Translation: CAA90864.1.
D82882 Genomic DNA. Translation: BAA11623.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZWX-ray2.70A/B1-313[»]
ProteinModelPortaliP52279.
SMRiP52279.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERixanca-impep. Proline_iminopeptidase.
MEROPSiS33.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP52279.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005944. Pro_iminopeptidase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006431. Pept_S33. 1 hit.
PRINTSiPR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01249. pro_imino_pep_1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPIP_XANCI
AccessioniPrimary (citable) accession number: P52279
Secondary accession number(s): P96186
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.