P0A3Z3 (AMPP2_STRCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Xaa-Pro aminopeptidase 2
EC=3.4.11.9

Alternative name(s):
Aminoacylproline aminopeptidase II
Aminopeptidase P II
Short name=APP
Short name=PEPP II
X-Pro aminopeptidase II
Xaa-Pro aminopeptidase II

Gene names

Name:	pepP2
Ordered Locus Names:	SCO1352
ORF Names:	2SCG61.34c

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces coelicolor

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the peptidase M24B family.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: InterPro metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 470	470	Xaa-Pro aminopeptidase 2		PRO_0000185080
Sites
	Metal binding	287	1	Manganese 2 By similarity
	Metal binding	299	1	Manganese 1 By similarity
	Metal binding	299	1	Manganese 2 By similarity
	Metal binding	382	1	Manganese 1 By similarity
	Metal binding	413	1	Manganese 1 By similarity
	Metal binding	437	1	Manganese 1 By similarity
	Metal binding	437	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A3Z3 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 0D3D33CE256523C2	FASTA	470	51,925
	10 20 30 40 50 60 MSNRRKNSLY PTLSAELSAL MRTGWADTER HDLAPAEQAP YAALRRAALS ARFPGERLVV 70 80 90 100 110 120 PSGNLKVRSN DDTYPFRSYS GYVHMTGDQA RDGALVLEPR PDGGHDAYCY QLPRDSRDDD 130 140 150 160 170 180 EFWTGAHAEL WTGRRRSLAE SERVLGLPCR DVRTAAADLA AVSEVRTRIV RGIDPALEAA 190 200 210 220 230 240 VTTDEERDAE LEDALSDLRL VKDAWELGEL RKAVDSTVRG FTDVVGELSR AVASSERWLE 250 260 270 280 290 300 GTFFRRARLE GNAVGYGTIC AAGEHATIMH WTDNDGPVRP GDLLLLDAGV ETRSLYTADV 310 320 330 340 350 360 TRTLPISGTF TPLQREVYDA VYEAQEAGIA TVKPGAAYRD FHEAAQRHLA ARLVEWGFIE 370 380 390 400 410 420 GPAERAYELG LQRRFTMAGT GHMLGLDVHD CARARTEEYV EGVLEPGMCL TVEPGLYFQA 430 440 450 460 470 DDLTVPEEWR GIGVRIEDDL VVTEDGHENL SAGLPRSADE VEAWMARFAG

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939108 Genomic DNA. Translation: CAB95809.1.
RefSeq	NP_625637.1. NC_003888.3.
3D structure databases
ProteinModelPortal	P0A3Z3.
ModBase	Search...
Protein-protein interaction databases
STRING	100226.SCO1352.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB95809; CAB95809; CAB95809.
GeneID	1096775.
KEGG	sco:SCO1352.
PATRIC	23732272. VBIStrCoe124346_1360.
Phylogenomic databases
eggNOG	COG0006.
HOGENOM	HOG000008761.
KO	K01262.
OMA	CARARTE.
ProtClustDB	CLSK902138.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR007865. Aminopep_P_N. 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]
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...

Entry information

Entry name

AMPP2_STRCO

Accession

Primary (citable) accession number: P0A3Z3
Secondary accession number(s): Q60394

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program