Reviewed, UniProtKB/Swiss-Prot P0AE18 (AMPM_ECOLI)

Names and origin

Protein names

Recommended name:
    Methionine aminopeptidase
      Short name=MAP
    EC=3.4.11.18
Alternative name(s):
    Peptidase M

Gene names

Name:	map
Ordered Locus Names:	b0168, JW0163

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	264 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)

Function	Removes the amino-terminal methionine from nascent proteins.
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Ref.10
Cofactor	Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions. Ref.7 Binds 1 sodium ion per subunit. The sodium ion has a structural role. Ref.7
Subunit structure	Monomer.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
gshB	P04425	1	EBI-553355,EBI-909107

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 264

263

Methionine aminopeptidase

PRO_0000148937

Sites

Metal binding

97

1

Cobalt 1

Metal binding

108

1

Cobalt 1

Metal binding

108

1

Cobalt 2

Metal binding

171

1

Cobalt 2

Metal binding

204

1

Cobalt 2

Metal binding

235

1

Cobalt 1

Metal binding

235

1

Cobalt 2

Binding site

79

1

Substrate

Binding site

99

1

Substrate

Binding site

178

1

Substrate

Experimental info

Mutagenesis

79

1

H → A: Reduces activity 100000-fold. Ref.7

Mutagenesis

178

1

H → A: Reduces activity 50-fold. Ref.7

Secondary structure

1

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264

Helix Strand Turn

Details...

Helix

8 – 28

21

Helix

29 – 31

3

Helix

38 – 51

14

Beta strand

56 – 59

4

Helix

62 – 64

3

Beta strand

67 – 73

7

Beta strand

76 – 78

3

Beta strand

93 – 102

10

Beta strand

105 – 114

10

Helix

120 – 139

20

Helix

146 – 159

14

Beta strand

170 – 172

3

Beta strand

174 – 183

10

Beta strand

200 – 203

4

Beta strand

206 – 210

5

Beta strand

214 – 216

3

Beta strand

223 – 225

3

Beta strand

231 – 233

3

Beta strand

235 – 240

6

Beta strand

242 – 249

8

Beta strand

258 – 261

4

Sequences

	Sequence		Length	Mass (Da)
	P0AE18-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: F2D0B57715A67851	FASTA	264	29,331
	10 20 30 40 50 60 MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL 70 80 90 100 110 120 GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI 130 140 150 160 170 180 MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE 190 200 210 220 230 240 PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV 250 260 TDNGCEILTL RKDDTIPAII SHDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure." Ben-Bassat A., Bauer K., Chang S.-Y., Myambo K., Boosman A., Chang S. J. Bacteriol. 169:751-757(1987) [PubMed: 3027045] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-64. Strain: K12.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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]	"Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme." Roderick S.L., Mathews B.W. Biochemistry 32:3907-3912(1993) [PubMed: 8471602] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[7]	"Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis." Lowther W.T., Orville A.M., Madden D.T., Lim S., Rich D.H., Matthews B.W. Biochemistry 38:7678-7688(1999) [PubMed: 10387007] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SODIUM; COBALT IONS AND INHIBITOR, COFACTOR, MUTAGENESIS OF HIS-79 AND HIS-178.
[8]	"Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues." Lowther W.T., Zhang Y., Sampson P.B., Honek J.F., Matthews B.W. Biochemistry 38:14810-14819(1999) [PubMed: 10555963] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; PRODUCT AND TRANSITION STATE ANALOGS.
[9]	"Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes." Ma Z.-Q., Xie S.-X., Huang Q.-Q., Nan F.-J., Hurley T.D., Ye Q.-Z. BMC Struct. Biol. 7:84-84(2007) [PubMed: 18093325] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 2-264 IN COMPLEXES WITH MANGANESE IONS AND INHIBITORS.
[10]	"Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors." Evdokimov A.G., Pokross M., Walter R.L., Mekel M., Barnett B.L., Amburgey J., Seibel W.L., Soper S.J., Djung J.F., Fairweather N., Diven C., Rastogi V., Grinius L., Klanke C., Siehnel R., Twinem T., Andrews R., Curnow A. Proteins 66:538-546(2007) [PubMed: 17120228] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 2-264 IN COMPLEXES WITH COBALT IONS; METHIONINE OR INHIBITORS OF THE PYRAZOLE DIAMINE TYPE, CATALYTIC ACTIVITY.
[11]	"Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II)-form selectivity and antibacterial activity." Wang W.-L., Chai S.C., Huang M., He H.-Z., Hurley T.D., Ye Q.-Z. J. Med. Chem. 51:6110-6120(2008) [PubMed: 18785729] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 4-264 IN COMPLEXES WITH CATECHOL-CONTAINING INHIBITORS AND IRON IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M15106 Genomic DNA. Translation: AAA24112.1.
U70214 Genomic DNA. Translation: AAB08597.1.
U00096 Genomic DNA. Translation: AAC73279.1.
AP009048 Genomic DNA. Translation: BAB96743.1.

PIR

DPECM. A27761.

RefSeq

AP_000828.1.
NP_414710.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C21	X-ray	1.80	A	2-264	[»]
1C22	X-ray	1.75	A	2-264	[»]
1C23	X-ray	2.00	A	2-264	[»]
1C24	X-ray	1.70	A	2-264	[»]
1C27	X-ray	1.95	A	2-264	[»]
1MAT	X-ray	2.40	A	1-264	[»]
1XNZ	X-ray	1.52	A	1-264	[»]
1YVM	X-ray	1.60	A	1-264	[»]
2BB7	X-ray	1.70	A	1-264	[»]
2EVC	X-ray	1.60	A	1-264	[»]
2EVM	X-ray	1.70	A	1-264	[»]
2EVO	X-ray	1.70	A/B	1-264	[»]
2GG0	X-ray	1.28	A	2-264	[»]
2GG2	X-ray	1.00	A	2-264	[»]
2GG3	X-ray	1.45	A	2-264	[»]
2GG5	X-ray	2.12	A	2-264	[»]
2GG7	X-ray	1.12	A	2-264	[»]
2GG8	X-ray	1.80	A	2-264	[»]
2GG9	X-ray	1.05	A	2-264	[»]
2GGB	X-ray	2.13	A	2-264	[»]
2GGC	X-ray	1.00	A	2-264	[»]
2GTX	X-ray	2.00	A/B	4-264	[»]
2GU4	X-ray	1.80	A/B	4-264	[»]
2GU5	X-ray	1.60	A/B	4-264	[»]
2GU6	X-ray	1.70	A/B	4-264	[»]
2GU7	X-ray	2.00	A/B	4-264	[»]
2MAT	X-ray	1.90	A	1-264	[»]
2P98	X-ray	1.70	A	2-263	[»]
2P99	X-ray	1.80	A	2-262	[»]
2P9A	X-ray	1.60	A	2-263	[»]
2Q92	X-ray	1.90	A	2-263	[»]
2Q93	X-ray	1.60	A	2-264	[»]
2Q94	X-ray	1.63	A	2-263	[»]
2Q95	X-ray	1.70	A	2-264	[»]
2Q96	X-ray	1.60	A	2-264	[»]
3D27	X-ray	2.20	A	4-264	[»]
3MAT	X-ray	2.00	A	1-264	[»]
4MAT	X-ray	2.00	A	1-264	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AE18. 25 interactions.

STRING

P0AE18.

Protein family/group databases

MEROPS

M24.001.

2-D gel databases

SWISS-2DPAGE

P0AE18.

ECO2DBASE

F029.7. 6TH EDITION.

Genome annotation databases

GeneID

947882.

GenomeReviews

Gene locus JW0163 in contig AP009048_GR.
Gene locus b0168 in contig U00096_GR.

KEGG

ecj:JW0163.
eco:b0168.

Organism-specific databases

EchoBASE

EB0565.

EcoGene

EG10570. map.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AE18.

OMA

VIQKHAE.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10570-MON.

Gene expression databases

Genevestigator

P0AE18.

Family and domain databases

InterPro

IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]

Gene3D

G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.

PANTHER

PTHR10804:SF13. Pept_M24A_MAP1. 1 hit.
PTHR10804. Peptidase_M24_cat_core. 1 hit.

Pfam

PF00557. Peptidase_M24. 1 hit.
[Graphical view]

PRINTS

PR00599. MAPEPTIDASE.

TIGRFAMs

TIGR00500. met_pdase_I. 1 hit.

PROSITE

PS00680. MAP_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P0AE18.

Entry information

Entry name

AMPM_ECOLI

Accession

Primary (citable) accession number: P0AE18
Secondary accession number(s): P07906

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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