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P15034

- AMPP_ECOLI

UniProt

P15034 - AMPP_ECOLI

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Protein

Xaa-Pro aminopeptidase

Gene

pepP

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.

Cofactori

Mn2+Note: Binds 2 manganese ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi261 – 2611Manganese 2
Metal bindingi272 – 2721Manganese 1
Metal bindingi272 – 2721Manganese 2
Metal bindingi355 – 3551Manganese 1
Metal bindingi384 – 3841Manganese 1
Metal bindingi407 – 4071Manganese 1
Metal bindingi407 – 4071Manganese 2

GO - Molecular functioni

  1. aminopeptidase activity Source: EcoCyc
  2. manganese ion binding Source: InterPro
  3. metalloexopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10697-MONOMER.
ECOL316407:JW2876-MONOMER.
MetaCyc:EG10697-MONOMER.

Protein family/group databases

MEROPSiM24.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Xaa-Pro aminopeptidase (EC:3.4.11.9)
Alternative name(s):
Aminoacylproline aminopeptidase
Aminopeptidase P II
Short name:
APP-II
X-Pro aminopeptidase
Gene namesi
Name:pepP
Ordered Locus Names:b2908, JW2876
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10697. pepP.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 441440Xaa-Pro aminopeptidasePRO_0000185075Add
BLAST

Proteomic databases

PaxDbiP15034.
PRIDEiP15034.

Expressioni

Gene expression databases

GenevestigatoriP15034.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
guaCP605602EBI-554801,EBI-544491

Protein-protein interaction databases

DIPiDIP-10459N.
IntActiP15034. 10 interactions.
MINTiMINT-1252312.
STRINGi511145.b2908.

Structurei

Secondary structure

1
441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1914Combined sources
Beta strandi22 – 298Combined sources
Beta strandi35 – 373Combined sources
Helixi48 – 547Combined sources
Beta strandi62 – 676Combined sources
Beta strandi69 – 713Combined sources
Beta strandi73 – 797Combined sources
Helixi84 – 907Combined sources
Helixi95 – 1039Combined sources
Beta strandi106 – 1105Combined sources
Helixi111 – 1133Combined sources
Helixi114 – 1229Combined sources
Beta strandi126 – 1294Combined sources
Helixi136 – 15015Combined sources
Helixi153 – 1553Combined sources
Beta strandi161 – 1644Combined sources
Helixi167 – 1759Combined sources
Helixi179 – 20224Combined sources
Helixi209 – 22214Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi233 – 2364Combined sources
Helixi237 – 2415Combined sources
Beta strandi257 – 2626Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi273 – 2786Combined sources
Helixi285 – 30420Combined sources
Helixi311 – 32818Combined sources
Helixi336 – 3416Combined sources
Turni342 – 3487Combined sources
Beta strandi358 – 3625Combined sources
Helixi369 – 3713Combined sources
Beta strandi380 – 3834Combined sources
Beta strandi386 – 3894Combined sources
Helixi397 – 3993Combined sources
Beta strandi402 – 4054Combined sources
Beta strandi407 – 4137Combined sources
Beta strandi416 – 4216Combined sources
Helixi428 – 43912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A16X-ray2.30A2-441[»]
1JAWX-ray2.70A2-441[»]
1M35X-ray2.40A/B/C/D/E/F2-441[»]
1N51X-ray2.30A2-441[»]
1W2MX-ray2.40A/B/C/D/E/F2-441[»]
1W7VX-ray2.00A/B/C/D2-441[»]
1WBQX-ray2.30A/B/C/D2-441[»]
1WL6X-ray2.00A2-441[»]
1WL9X-ray1.90A2-441[»]
1WLRX-ray2.10A2-441[»]
2BH3X-ray2.40A2-441[»]
2BHAX-ray2.40A2-441[»]
2BHBX-ray2.41A2-441[»]
2BHCX-ray2.40A2-441[»]
2BHDX-ray2.50A2-441[»]
2BN7X-ray2.40A2-441[»]
2BWSX-ray1.75A2-441[»]
2BWTX-ray2.90A2-441[»]
2BWUX-ray2.20A2-441[»]
2BWVX-ray1.70A2-441[»]
2BWWX-ray2.61A2-441[»]
2BWXX-ray1.70A2-441[»]
2BWYX-ray2.40A2-441[»]
2V3XX-ray1.70A2-441[»]
2V3YX-ray1.60A2-441[»]
2V3ZX-ray1.56A2-441[»]
ProteinModelPortaliP15034.
SMRiP15034. Positions 2-441.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15034.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24B family.Curated

Phylogenomic databases

eggNOGiCOG0006.
HOGENOMiHOG000008762.
InParanoidiP15034.
KOiK01262.
OMAiHDVGHYG.
OrthoDBiEOG6XHC3N.
PhylomeDBiP15034.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR007865. Aminopep_P_N.
IPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamiPF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SMARTiSM01011. AMP_N. 1 hit.
[Graphical view]
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15034-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF
60 70 80 90 100
WYFTGFNEPE AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP
110 120 130 140 150
EKLGVDRALA FSEINQQLYQ LLNGLDVVYH AQGEYAYADV IVNSALEKLR
160 170 180 190 200
KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE EIAVLRRAGE ITAMAHTRAM
210 220 230 240 250
EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG CILHYTENEC
260 270 280 290 300
EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET
310 320 330 340 350
SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM
360 370 380 390 400
HGLSHWLGLD VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR
410 420 430 440
GIGIRIEDDI VITETGNENL TASVVKKPEE IEALMVAARK Q
Length:441
Mass (Da):49,815
Last modified:January 23, 2007 - v2
Checksum:i80A6A5BDD86D84B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00398 Genomic DNA. Translation: BAA00299.1.
D90281 Genomic DNA. Translation: BAA14325.1.
U28377 Genomic DNA. Translation: AAA69076.1.
U00096 Genomic DNA. Translation: AAC75946.1.
AP009048 Genomic DNA. Translation: BAE76973.1.
PIRiJX0067. DPECP.
RefSeqiNP_417384.1. NC_000913.3.
YP_491109.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75946; AAC75946; b2908.
BAE76973; BAE76973; BAE76973.
GeneIDi12930242.
947385.
KEGGiecj:Y75_p2840.
eco:b2908.
PATRICi32121230. VBIEscCol129921_3003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00398 Genomic DNA. Translation: BAA00299.1 .
D90281 Genomic DNA. Translation: BAA14325.1 .
U28377 Genomic DNA. Translation: AAA69076.1 .
U00096 Genomic DNA. Translation: AAC75946.1 .
AP009048 Genomic DNA. Translation: BAE76973.1 .
PIRi JX0067. DPECP.
RefSeqi NP_417384.1. NC_000913.3.
YP_491109.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A16 X-ray 2.30 A 2-441 [» ]
1JAW X-ray 2.70 A 2-441 [» ]
1M35 X-ray 2.40 A/B/C/D/E/F 2-441 [» ]
1N51 X-ray 2.30 A 2-441 [» ]
1W2M X-ray 2.40 A/B/C/D/E/F 2-441 [» ]
1W7V X-ray 2.00 A/B/C/D 2-441 [» ]
1WBQ X-ray 2.30 A/B/C/D 2-441 [» ]
1WL6 X-ray 2.00 A 2-441 [» ]
1WL9 X-ray 1.90 A 2-441 [» ]
1WLR X-ray 2.10 A 2-441 [» ]
2BH3 X-ray 2.40 A 2-441 [» ]
2BHA X-ray 2.40 A 2-441 [» ]
2BHB X-ray 2.41 A 2-441 [» ]
2BHC X-ray 2.40 A 2-441 [» ]
2BHD X-ray 2.50 A 2-441 [» ]
2BN7 X-ray 2.40 A 2-441 [» ]
2BWS X-ray 1.75 A 2-441 [» ]
2BWT X-ray 2.90 A 2-441 [» ]
2BWU X-ray 2.20 A 2-441 [» ]
2BWV X-ray 1.70 A 2-441 [» ]
2BWW X-ray 2.61 A 2-441 [» ]
2BWX X-ray 1.70 A 2-441 [» ]
2BWY X-ray 2.40 A 2-441 [» ]
2V3X X-ray 1.70 A 2-441 [» ]
2V3Y X-ray 1.60 A 2-441 [» ]
2V3Z X-ray 1.56 A 2-441 [» ]
ProteinModelPortali P15034.
SMRi P15034. Positions 2-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10459N.
IntActi P15034. 10 interactions.
MINTi MINT-1252312.
STRINGi 511145.b2908.

Protein family/group databases

MEROPSi M24.004.

Proteomic databases

PaxDbi P15034.
PRIDEi P15034.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75946 ; AAC75946 ; b2908 .
BAE76973 ; BAE76973 ; BAE76973 .
GeneIDi 12930242.
947385.
KEGGi ecj:Y75_p2840.
eco:b2908.
PATRICi 32121230. VBIEscCol129921_3003.

Organism-specific databases

EchoBASEi EB0691.
EcoGenei EG10697. pepP.

Phylogenomic databases

eggNOGi COG0006.
HOGENOMi HOG000008762.
InParanoidi P15034.
KOi K01262.
OMAi HDVGHYG.
OrthoDBi EOG6XHC3N.
PhylomeDBi P15034.

Enzyme and pathway databases

BioCyci EcoCyc:EG10697-MONOMER.
ECOL316407:JW2876-MONOMER.
MetaCyc:EG10697-MONOMER.

Miscellaneous databases

EvolutionaryTracei P15034.
PROi P15034.

Gene expression databases

Genevestigatori P15034.

Family and domain databases

Gene3Di 3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProi IPR007865. Aminopep_P_N.
IPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view ]
Pfami PF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SMARTi SM01011. AMP_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and high expression of aminopeptidase P gene from Escherichia coli HB101."
    Yoshimoto T., Tone H., Honda T., Osatomi K., Kobayashi R., Tsuru D.
    J. Biochem. 105:412-416(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, CHARACTERIZATION.
    Strain: ATCC 33694 / HB101.
  2. "Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone."
    Nakahigashi K., Miyamoto K., Nishimura K., Inokuchi H.
    J. Bacteriol. 174:7352-7359(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33694 / HB101.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli."
    Wilce M.C.J., Bond C.S., Dixon N.E., Freeman H.C., Guss J.M., Lilley P.E., Wilce J.A.
    Proc. Natl. Acad. Sci. U.S.A. 95:3472-3477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiAMPP_ECOLI
AccessioniPrimary (citable) accession number: P15034
Secondary accession number(s): Q2M9T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 150 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3