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Protein

Methionine aminopeptidase 2

Gene

mapB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.1 PublicationUniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761SubstrateUniRule annotation
Metal bindingi94 – 941Divalent metal cation 1UniRule annotation
Metal bindingi105 – 1051Divalent metal cation 1UniRule annotation
Metal bindingi105 – 1051Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei175 – 1751SubstrateUniRule annotation
Metal bindingi202 – 2021Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
Metal bindingi233 – 2331Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU07690-MONOMER.

Protein family/group databases

MEROPSiM24.036.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP 2UniRule annotation
Short name:
MetAP 2UniRule annotation
Gene namesi
Name:mapBUniRule annotation
Synonyms:yflG
Ordered Locus Names:BSU07690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU07690. [Micado]

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Methionine aminopeptidase 2PRO_0000361275Add
BLAST

Proteomic databases

PaxDbiO34484.

Expressioni

Inductioni

Expressed at very low levels throughout growth.1 Publication

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi224308.BSU07690.

Structurei

3D structure databases

ProteinModelPortaliO34484.
SMRiO34484. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030426.
InParanoidiO34484.
KOiK01265.
OMAiLELMITN.
OrthoDBiEOG6MWNDS.
PhylomeDBiO34484.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.

Sequencei

Sequence statusi: Complete.

O34484-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIVTNDQELE GLKKIGRIVA LAREEMKRKA EPGMSTKDLD LIGKAVLDEH
60 70 80 90 100
GAVSAPEKEY DFPGVTCISV NDEVAHGIPS TSKILKAGDL VNIDISAEFG
110 120 130 140 150
GFYSDTGISF VLGEGEERLH KLCQCAENAF QKGLQQAKAG KRQNQIGRAV
160 170 180 190 200
YHEARSQGFT VIKTLTGHGI GRSLHEAPNH IMNYYDPFDN ALFKNGTVIA
210 220 230 240
LEPFISTKAE TIVEAGDGWT FKTPDKSMVA QVEHTIVITK DEPIILTKL
Length:249
Mass (Da):27,211
Last modified:January 1, 1998 - v1
Checksum:iC3C36DE944528E3E
GO

Mass spectrometryi

Molecular mass is 27209.35±2.14 Da from positions 1 - 249. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86417 Genomic DNA. Translation: BAA22300.1.
AL009126 Genomic DNA. Translation: CAB12598.1.
PIRiE69810.
RefSeqiNP_388650.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12598; CAB12598; BSU07690.
GeneIDi936121.
KEGGibsu:BSU07690.
PATRICi18973190. VBIBacSub10457_0809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86417 Genomic DNA. Translation: BAA22300.1.
AL009126 Genomic DNA. Translation: CAB12598.1.
PIRiE69810.
RefSeqiNP_388650.1. NC_000964.3.

3D structure databases

ProteinModelPortaliO34484.
SMRiO34484. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU07690.

Protein family/group databases

MEROPSiM24.036.

Proteomic databases

PaxDbiO34484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12598; CAB12598; BSU07690.
GeneIDi936121.
KEGGibsu:BSU07690.
PATRICi18973190. VBIBacSub10457_0809.

Organism-specific databases

GenoListiBSU07690. [Micado]

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030426.
InParanoidiO34484.
KOiK01265.
OMAiLELMITN.
OrthoDBiEOG6MWNDS.
PhylomeDBiO34484.

Enzyme and pathway databases

BioCyciBSUB:BSU07690-MONOMER.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MASS SPECTROMETRY, COFACTOR, INDUCTION, SUBCELLULAR LOCATION.
    Strain: 168.

Entry informationi

Entry nameiMAP12_BACSU
AccessioniPrimary (citable) accession number: O34484
Secondary accession number(s): Q79ET8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.