O34484 (AMPM2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 2
Short name=MAP 2
EC=3.4.11.18

Gene names

Name:	mapB
Synonyms:	yflG
Ordered Locus Names:	BSU07690

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
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.
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. Ref.3
Subcellular location	Cytoplasm Ref.3.
Induction	Expressed at very low levels throughout growth. Ref.3
Sequence similarities	Belongs to the peptidase M24A family.
Mass spectrometry	Molecular mass is 27209.35±2.14 Da from positions 1 - 249. Ref.3

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase 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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 249	249	Methionine aminopeptidase 2		PRO_0000361275
Sites
	Metal binding	94	1	Cobalt 1 By similarity
	Metal binding	105	1	Cobalt 1 By similarity
	Metal binding	105	1	Cobalt 2 By similarity
	Metal binding	168	1	Cobalt 2 By similarity
	Metal binding	202	1	Cobalt 2 By similarity
	Metal binding	233	1	Cobalt 1 By similarity
	Metal binding	233	1	Cobalt 2 By similarity
	Binding site	76	1	Substrate By similarity
	Binding site	175	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O34484 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C3C36DE944528E3E	FASTA	249	27,211
	10 20 30 40 50 60 MIVTNDQELE GLKKIGRIVA LAREEMKRKA EPGMSTKDLD LIGKAVLDEH GAVSAPEKEY 70 80 90 100 110 120 DFPGVTCISV NDEVAHGIPS TSKILKAGDL VNIDISAEFG GFYSDTGISF VLGEGEERLH 130 140 150 160 170 180 KLCQCAENAF QKGLQQAKAG KRQNQIGRAV YHEARSQGFT VIKTLTGHGI GRSLHEAPNH 190 200 210 220 230 240 IMNYYDPFDN ALFKNGTVIA LEPFISTKAE TIVEAGDGWT FKTPDKSMVA QVEHTIVITK DEPIILTKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of the Bacillus subtilis genome reveal genes for a new two-component system, three spore germination proteins, an iron uptake system and a general stress response protein." Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J. Gene 194:191-199(1997) [PubMed: 9272861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / AC327.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis." You C., Lu H., Sekowska A., Fang G., Wang Y., Gilles A.-M., Danchin A. BMC Microbiol. 5:57-57(2005) [PubMed: 16207374] [Abstract] Cited for: CHARACTERIZATION, MASS SPECTROMETRY, COFACTOR, INDUCTION, SUBCELLULAR LOCATION. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D86417 Genomic DNA. Translation: BAA22300.1. AL009126 Genomic DNA. Translation: CAB12598.1.
PIR	E69810.
RefSeq	NP_388650.1. NC_000964.3.
3D structure databases
HSSP	HSSP built from PDB template 1QXY based on UniProtKB P0A078.
ProteinModelPortal	O34484.
SMR	O34484. Positions 1-249.
ModBase	Search...
Protein family/group databases
MEROPS	M24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002347; EBBACP00000002347; EBBACG00000002342.
GeneID	936121.
GenomeReviews	Gene locus BSU07690 in contig AL009126_GR.
KEGG	bsu:BSU07690.
NMPDR	fig|224308.1.peg.769.
PATRIC	18973190. VBIBacSub10457_0809.
Organism-specific databases
GenoList	BSU07690. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000031874.
HOGENOM	HBG299384.
OMA	VFTVEPF.
PhylomeDB	O34484.
ProtClustDB	PRK12896.
Enzyme and pathway databases
BioCyc	BSUB:BSU07690-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.
ProtoNet	Search...

Entry information

Entry name

AMPM2_BACSU

Accession

Primary (citable) accession number: O34484
Secondary accession number(s): Q79ET8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program