P15034 (AMPP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	pepP
Ordered Locus Names:	b2908, JW2876

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Cofactor	Binds 2 manganese ions per subunit.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the peptidase M24B family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	aminopeptidase activity Inferred from direct assay PubMed 2851590. Source: EcoCyc manganese ion binding Inferred from electronic annotation. Source: InterPro metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
guaC	P60560	2	EBI-554801,EBI-544491

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 441

440

Xaa-Pro aminopeptidase

PRO_0000185075

Sites

Metal binding

261

1

Manganese 2

Metal binding

272

1

Manganese 1

Metal binding

272

1

Manganese 2

Metal binding

355

1

Manganese 1

Metal binding

384

1

Manganese 1

Metal binding

407

1

Manganese 1

Metal binding

407

1

Manganese 2

Secondary structure

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441

Helix Strand Turn

Details...

Helix

6 – 19

14

Beta strand

22 – 29

8

Beta strand

35 – 37

3

Helix

48 – 54

7

Beta strand

62 – 67

6

Beta strand

69 – 71

3

Beta strand

73 – 79

7

Helix

84 – 90

7

Helix

95 – 103

9

Beta strand

106 – 110

5

Helix

111 – 113

3

Helix

114 – 122

9

Beta strand

126 – 129

4

Helix

136 – 150

15

Helix

153 – 155

3

Beta strand

161 – 164

4

Helix

167 – 175

9

Helix

179 – 202

24

Helix

209 – 222

14

Beta strand

227 – 230

4

Beta strand

233 – 236

4

Helix

237 – 241

5

Beta strand

257 – 262

6

Beta strand

264 – 266

3

Beta strand

273 – 278

6

Helix

285 – 304

20

Helix

311 – 328

18

Helix

336 – 341

6

Turn

342 – 348

7

Beta strand

358 – 362

5

Helix

369 – 371

3

Beta strand

380 – 383

4

Beta strand

386 – 389

4

Helix

397 – 399

3

Beta strand

402 – 405

4

Beta strand

407 – 413

7

Beta strand

416 – 421

6

Helix

428 – 439

12

Sequences

	Sequence		Length	Mass (Da)
	P15034 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 80A6A5BDD86D84B1	FASTA	441	49,815
	10 20 30 40 50 60 MSEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF WYFTGFNEPE 70 80 90 100 110 120 AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP EKLGVDRALA FSEINQQLYQ 130 140 150 160 170 180 LLNGLDVVYH AQGEYAYADV IVNSALEKLR KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE 190 200 210 220 230 240 EIAVLRRAGE ITAMAHTRAM EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG 250 260 270 280 290 300 CILHYTENEC EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET 310 320 330 340 350 360 SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM HGLSHWLGLD 370 380 390 400 410 420 VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR GIGIRIEDDI VITETGNENL 430 440 TASVVKKPEE IEALMVAARK Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

DPECP. JX0067.

RefSeq

NP_417384.1. NC_000913.2.
YP_491109.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-440	[»]
1N51	X-ray	2.30	A	2-440	[»]
1W2M	X-ray	2.40	A/B/C/D/E/F	2-441	[»]
1W7V	X-ray	2.00	A/B/C/D	2-440	[»]
1WBQ	X-ray	2.30	A/B/C/D	2-440	[»]
1WL6	X-ray	2.00	A	2-440	[»]
1WL9	X-ray	1.90	A	2-440	[»]
1WLR	X-ray	2.10	A	2-440	[»]
2BH3	X-ray	2.40	A	2-440	[»]
2BHA	X-ray	2.40	A	2-440	[»]
2BHB	X-ray	2.41	A	2-440	[»]
2BHC	X-ray	2.40	A	2-440	[»]
2BHD	X-ray	2.50	A	2-440	[»]
2BN7	X-ray	2.40	A	2-440	[»]
2BWS	X-ray	1.75	A	2-441	[»]
2BWT	X-ray	2.90	A	2-440	[»]
2BWU	X-ray	2.20	A	2-440	[»]
2BWV	X-ray	1.70	A	2-441	[»]
2BWW	X-ray	2.61	A	2-440	[»]
2BWX	X-ray	1.70	A	2-440	[»]
2BWY	X-ray	2.40	A	2-440	[»]
2V3X	X-ray	1.70	A	2-440	[»]
2V3Y	X-ray	1.60	A	2-440	[»]
2V3Z	X-ray	1.56	A	2-440	[»]

ProteinModelPortal

P15034.

SMR

P15034. Positions 2-441.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10459N.

IntAct

P15034. 10 interactions.

MINT

MINT-1252312.

STRING

511145.b2908.

Protein family/group databases

MEROPS

M24.004.

Proteomic databases

PaxDb

P15034.

PRIDE

P15034.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75946; AAC75946; b2908.
BAE76973; BAE76973; BAE76973.

GeneID

12930242.
947385.

KEGG

ecj:Y75_p2840.
eco:b2908.

PATRIC

32121230. VBIEscCol129921_3003.

Organism-specific databases

EchoBASE

EB0691.

EcoGene

EG10697. pepP.

Phylogenomic databases

eggNOG

COG0006.

HOGENOM

HOG000008762.

KO

K01262.

OMA

VRAMQAC.

ProtClustDB

PRK10879.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P15034.

Family and domain databases

Gene3D

3.90.230.10. 1 hit.

InterPro

IPR007865. Aminopep_P_N.
IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]

Pfam

PF05195. AMP_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]

PRINTS

PR00599. MAPEPTIDASE.

SMART

SM01011. AMP_N. 1 hit.
[Graphical view]

SUPFAM

SSF55920. Peptidase_M24_cat_core. 1 hit.

PROSITE

PS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P15034.

Entry information

Entry name

AMPP_ECOLI

Accession

Primary (citable) accession number: P15034
Secondary accession number(s): Q2M9T3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program