P19994 (AMPM1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 1
Short name=MAP 1
EC=3.4.11.18

Alternative name(s):
Peptidase M

Gene names

Name:	map
Ordered Locus Names:	BSU01380

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	248 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. Ref.4
Subcellular location	Cytoplasm Ref.4.
Induction	Expression increases gradually during the log phase of growth. Ref.4
Sequence similarities	Belongs to the peptidase M24A family.
Mass spectrometry	Molecular mass is 27409.17±0.92 Da from positions 1 - 248. Ref.4

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 – 248	248	Methionine aminopeptidase 1		PRO_0000148927
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	201	1	Cobalt 2 By similarity
	Metal binding	232	1	Cobalt 1 By similarity
	Metal binding	232	1	Cobalt 2 By similarity
	Binding site	77	1	Substrate By similarity
	Binding site	175	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19994 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 6D6F7A593D84A761	FASTA	248	27,409
	10 20 30 40 50 60 MIICKTPREL GIMREAGRIV ALTHEELKKH IKPGISTKEL DQIAERFIKK QGAIPSFKGY 70 80 90 100 110 120 NGFRGSICVS VNEELVHGIP GSRVLKDGDI ISIDIGAKLN GYHGDSAWTY PVGNISDDDK 130 140 150 160 170 180 KLLEVTEESL YKGLQEAKPG ERLSNISHAI QTYVENEQFS VVREYVGHGV GQDLHEDPQI 190 200 210 220 230 240 PHYGPPNKGP RLKPGMVLAI EPMVNAGSRY VKTLADNWTV VTVDGKKCAH FEHTIAITET GFDILTRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a Bacillus subtilis gene homologous to E. coli secY." Nakamura K., Nakamura A., Takamatsu H., Yoshikawa H., Yamane K. J. Biochem. 107:603-607(1990) [PubMed: 2113521] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genetic and transcriptional organization of the Bacillus subtilis spc-alpha region." Suh J.-W., Boylan S.A., Oh S.H., Price C.W. Gene 169:17-23(1996) [PubMed: 8635744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[3]	"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.
[4]	"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	D00619 Genomic DNA. Translation: BAA00497.1. L47971 Genomic DNA. Translation: AAB06821.1. AL009126 Genomic DNA. Translation: CAB11914.1.
PIR	JS0493.
RefSeq	NP_388019.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P19994.
SMR	P19994. Positions 1-247.
ModBase	Search...
Protein family/group databases
MEROPS	M24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002549; EBBACP00000002549; EBBACG00000002544.
GeneID	938929.
GenomeReviews	Gene locus BSU01380 in contig AL009126_GR.
KEGG	bsu:BSU01380.
NMPDR	fig|224308.1.peg.138.
PATRIC	18971785. VBIBacSub10457_0141.
Organism-specific databases
GenoList	BSU01380. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000031874.
HOGENOM	HBG299384.
OMA	CEILTDR.
PhylomeDB	P19994.
ProtClustDB	PRK05716.
Enzyme and pathway databases
BioCyc	BSUB:BSU01380-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...

Entry information

Entry name

AMPM1_BACSU

Accession

Primary (citable) accession number: P19994

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program