P0AE21 (AMPM_SHIFL) Reviewed, UniProtKB/Swiss-Prot

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:	SF0158, S0161

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins By similarity.
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
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 By similarity. Binds 1 sodium ion per subunit. The sodium ion has a structural role By similarity.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 264	264	Methionine aminopeptidase		PRO_0000148953
Sites
	Metal binding	97	1	Cobalt 1 By similarity
	Metal binding	108	1	Cobalt 1 By similarity
	Metal binding	108	1	Cobalt 2 By similarity
	Metal binding	171	1	Cobalt 2 By similarity
	Metal binding	204	1	Cobalt 2 By similarity
	Metal binding	235	1	Cobalt 1 By similarity
	Metal binding	235	1	Cobalt 2 By similarity
	Binding site	79	1	Substrate By similarity
	Binding site	178	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AE21 [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

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005674 Genomic DNA. Translation: AAN41820.1. AE014073 Genomic DNA. Translation: AAP15701.1.
RefSeq	NP_706113.1. NC_004337.2. NP_835896.1. NC_004741.1.
3D structure databases
ProteinModelPortal	P0AE21.
SMR	P0AE21. Positions 2-264.
ModBase	Search...
Protein family/group databases
MEROPS	M24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000087897; EBESCP00000084719; EBESCG00000086942. EBESCT00000090704; EBESCP00000087340; EBESCG00000089748.
GeneID	1024468. 1076594.
GenomeReviews	Gene locus SF0158 in contig AE005674_GR. Gene locus S0161 in contig AE014073_GR.
KEGG	sfl:SF0158. sfx:S0161.
PATRIC	18701270. VBIShiFle31049_0176.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010664.
HOGENOM	HBG299384.
OMA	ENGCEIM.
ProtClustDB	PRK05716.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN41820.1-MONOMER.
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.
KO	K01265.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00500. Met_pdase_I. 1 hit.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P0AE21.

Entry information

Entry name

AMPM_SHIFL

Accession

Primary (citable) accession number: P0AE21
Secondary accession number(s): P07906

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	January 25, 2012
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