Aminopeptidase N - Escherichia coli (strain K12)

Names and origin

Protein names

Recommended name:
    Aminopeptidase N
    EC=3.4.11.2
Alternative name(s):
    Alpha-aminoacylpeptide hydrolase

Gene names

Name:	pepN
Ordered Locus Names:	b0932, JW0915

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	870 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.
Catalytic activity	Release of an N-terminal amino acid, Xaa-\|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence similarities	Belongs to the peptidase M1 family.

Hide | Top

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aminopeptidase activity Inferred from direct assay. Source: UniProtKB metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.7

Chain

2 – 870

869

Aminopeptidase N

PRO_0000095069

Sites

Active site

298

1

By similarity

Active site

381

1

Proton donor Potential

Metal binding

297

1

Zinc; catalytic By similarity

Metal binding

301

1

Zinc; catalytic By similarity

Metal binding

320

1

Zinc; catalytic By similarity

Experimental info

Sequence conflict

76

1

E → D in CAA27647. Ref.7

Secondary structure

1

.

870

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P04825-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7C18C6BD8F2E5131
Show »

FASTA

870

98,919

        10         20         30         40         50         60 
MTQQPQAKYR HDYRAPDYQI TDIDLTFDLD AQKTVVTAVS QAVRHGASDA PLRLNGEDLK 

        70         80         90        100        110        120 
LVSVHINDEP WTAWKEEEGA LVISNLPERF TLKIINEISP AANTALEGLY QSGDALCTQC 

       130        140        150        160        170        180 
EAEGFRHITY YLDRPDVLAR FTTKIIADKI KYPFLLSNGN RVAQGELENG RHWVQWQDPF 

       190        200        210        220        230        240 
PKPCYLFALV AGDFDVLRDT FTTRSGREVA LELYVDRGNL DRAPWAMTSL KNSMKWDEER 

       250        260        270        280        290        300 
FGLEYDLDIY MIVAVDFFNM GAMENKGLNI FNSKYVLART DTATDKDYLD IERVIGHEYF 

       310        320        330        340        350        360 
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RINNVRTMRG LQFAEDASPM 

       370        380        390        400        410        420 
AHPIRPDMVI EMNNFYTLTV YEKGAEVIRM IHTLLGEENF QKGMQLYFER HDGSAATCDD 

       430        440        450        460        470        480 
FVQAMEDASN VDLSHFRRWY SQSGTPIVTV KDDYNPETEQ YTLTISQRTP ATPDQAEKQP 

       490        500        510        520        530        540 
LHIPFAIELY DNEGKVIPLQ KGGHPVNSVL NVTQAEQTFV FDNVYFQPVP ALLCEFSAPV 

       550        560        570        580        590        600 
KLEYKWSDQQ LTFLMRHARN DFSRWDAAQS LLATYIKLNV ARHQQGQPLS LPVHVADAFR 

       610        620        630        640        650        660 
AVLLDEKIDP ALAAEILTLP SVNEMAELFD IIDPIAIAEV REALTRTLAT ELADELLAIY 

       670        680        690        700        710        720 
NANYQSEYRV EHEDIAKRTL RNACLRFLAF GETHLADVLV SKQFHEANNM TDALAALSAA 

       730        740        750        760        770        780 
VAAQLPCRDA LMQEYDDKWH QNGLVMDKWF ILQATSPAAN VLETVRGLLQ HRSFTMSNPN 

       790        800        810        820        830        840 
RIRSLIGAFA GSNPAAFHAE DGSGYLFLVE MLTDLNSRNP QVASRLIEPL IRLKRYDAKR 

       850        860        870 
QEKMRAALEQ LKGLENLSGD LYEKITKALA

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli." Foglino M., Gharbi S., Lazdunski A. Gene 49:303-309(1986) [PubMed: 2436977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of the pepN gene and its over-expression in Escherichia coli." McCaman M.T., Gabe J.D. Gene 48:145-153(1986) [PubMed: 3549459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Sequence of the promoter and 5' coding region of pepN, and the amino-terminus of peptidase N from Escherichia coli K-12." McCaman M.T., Gabe J.D. Mol. Gen. Genet. 204:148-152(1986) [PubMed: 3018440] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242. Strain: K12.
[7]	"Nucleotide sequence of the promoter and amino-terminal encoding region of the Escherichia coli pepN gene." Bally M., Foglino M., Bruschi M., Murgier M., Lazdunski A. Eur. J. Biochem. 155:565-569(1986) [PubMed: 2869947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177, PROTEIN SEQUENCE OF 2-22.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04020 Genomic DNA. Translation: CAA27647.1.
X03709 Genomic DNA. Translation: CAA27336.1.
M15676 Genomic DNA. Translation: AAA24318.1.
U00096 Genomic DNA. Translation: AAC74018.1.
AP009048 Genomic DNA. Translation: BAA35684.1.
M15273 Genomic DNA. Translation: AAA24317.1.

PIR

DPECN. C64833.

RefSeq

AP_001562.1.
NP_415452.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DQ6	X-ray	1.50	A	1-870	[»]
2DQM	X-ray	1.60	A	1-870	[»]
2HPO	X-ray	1.65	A	2-869	[»]
2HPT	X-ray	2.30	A	2-869	[»]
2ZXG	X-ray	1.55	A	1-870	[»]
3B2P	X-ray	2.00	A	1-870	[»]
3B2X	X-ray	1.50	A	1-870	[»]
3B34	X-ray	1.30	A	1-870	[»]
3B37	X-ray	1.70	A	1-870	[»]
3B3B	X-ray	1.85	A	1-870	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10458N.

STRING

P04825.

Protein family/group databases

MEROPS

M01.005.

Genome annotation databases

GeneID

947253.

GenomeReviews

Gene locus JW0915 in contig AP009048_GR.
Gene locus b0932 in contig U00096_GR.

KEGG

ecj:JW0915.
eco:b0932.

Organism-specific databases

EchoBASE

EB0690.

EcoGene

EG10696. pepN.

CMR

Search...

Phylogenomic databases

eggNOG

COG0308.

HOGENOM

HBG289207.

OMA

EYFHNWS.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10696-MONOMER.
ECOL168927:B0932-MONOMER.

Gene expression databases

Genevestigator

P04825.

Family and domain databases

InterPro

IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
IPR012779. Peptidase_M1_pepN.
[Graphical view]

PANTHER

PTHR11533:SF8. Pept_M1_pepN. 1 hit.
PTHR11533. Peptidase_M1. 1 hit.

Pfam

PF01433. Peptidase_M1. 1 hit.
[Graphical view]

PRINTS

PR00756. ALADIPTASE.

TIGRFAMs

TIGR02414. pepN_proteo. 1 hit.

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Hide | Top

Entry information

Entry name

AMPN_ECOLI

Accession

Primary (citable) accession number: P04825

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top