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⊟Summary[edit | edit source]
- pan ID?: SAUPAN004903000
- symbol?: map
- synonym:
- description?: methionine aminopeptidase
- methionine aminopeptidase
- type I methionyl aminopeptidase
- methionine aminopeptidase 1
- M24 family methionyl aminopeptidase
- methionine aminopeptidase, type I
- putative metallopeptidase
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5098222..5098938
- synteny block?: BlockID0038090
- occurrence?: in 100% of 34 strains
map : methionine aminopeptidase [1]
• A crystal structure is available: 1QXW
While all bacterial coding sequences initiate with a formyl-methionine, not all ribosomal proteins contain an N-terminal formyl-methionine or methionine. After initial processing by peptide deformylase, methionine aminopeptidases cleave N-terminal methionine residues from nascent ribosomal proteins as they are emerging from the ribosome. Typically, the amino acid following the methionine (the P1' position) is small and uncharged to promote efficient cleavage. Large or polar P1' residues and/or proline at P2' block methionine aminopeptidase resulting in proteins retaining an N-terminal methionine.
⊟Orthologs[edit | edit source]
04-02981:
SA2981_1844 (map)
08BA02176:
C248_1960
11819-97:
MS7_1923
6850:
RSAU_001775 (mapB)
71193:
ST398NM01_1981
ECT-R 2:
ECTR2_1759 (map)
ED133:
SAOV_1986
ED98:
SAAV_1953
HO 5096 0412:
SAEMRSA15_17950
JH1:
SaurJH1_1976
JH9:
SaurJH9_1942
JKD6008:
SAA6008_01908
JKD6159:
SAA6159_01819
JSNZ:
JSNZ_001917 (map)
LGA251:
SARLGA251_17700
M013:
M013TW_1924
MRSA252:
SAR1978
MSHR1132:
SAMSHR1132_17330
MSSA476:
SAS1810
Mu3:
SAHV_1873 (map)
Mu50:
SAV1888 (map)
MW2:
MW1828 (map)
RF122:
SAB1820c
ST398:
SAPIG1981 (map)
T0131:
SAT0131_02012
TCH60:
HMPREF0772_11256 (map2)
TW20:
SATW20_18820
USA300_TCH1516:
USA300HOU_1884 (map)
VC40:
SAVC_08695
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEYGAISAPIHDE
N315 MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEYGAISAPIHDE
NCTC8325 MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEYGAISAPIHDE
Newman MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEYGAISAPIHDE
USA300_FPR3757 MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEYGAISAPIHDE
************************************************************
COL NFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNGYYADTGISFVVGESDDPMKQ
N315 NFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNGYYADTGISFVVGESDDPMKQ
NCTC8325 NFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNGYYADTGISFVVGESDDPMKQ
Newman NFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNGYYADTGISFVVGESDDPMKQ
USA300_FPR3757 NFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNGYYADTGISFVVGESDDPMKQ
************************************************************
COL KVCDVATMAFENAIAKVKPGTKLSNIGKAVHNTARQNDLKVIKNLTGHGVGLSLHEAPAH
N315 KVCDVATMAFENAIAKVKPGTKLSNIGKAVHNTARQNDLKVIKNLTGHGVGLSLHEAPAH
NCTC8325 KVCDVATMAFENAIAKVKPGTKLSNIGKAVHNTARQNDLKVIKNLTGHGVGLSLHEAPAH
Newman KVCDVATMAFENAIAKVKPGTKLSNIGKAVHNTARQNDLKVIKNLTGHGVGLSLHEAPAH
USA300_FPR3757 KVCDVATMAFENAIAKVKPGTKLSNIGKAVHNTARQNDLKVIKNLTGHGVGLSLHEAPAH
************************************************************
COL VLNYFDPKDKTLLTEGMVLAIEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTK
N315 VLNYFDPKDKTLLTEGMVLAIEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTK
NCTC8325 VLNYFDPKDKTLLTEGMVLAIEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTK
Newman VLNYFDPKDKTLLTEGMVLAIEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTK
USA300_FPR3757 VLNYFDPKDKTLLTEGMVLAIEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTK
************************************************************
COL DGPILTTKIEEE
N315 DGPILTTKIEEE
NCTC8325 DGPILTTKIEEE
Newman DGPILTTKIEEE
USA300_FPR3757 DGPILTTKIEEE
************
- ↑ Christian Oefner, Alice Douangamath, Allan D'Arcy, Sascha Häfeli, Daniel Mareque, Aengus Mac Sweeney, Juan Padilla, Sabine Pierau, Henk Schulz, Michael Thormann, Sjoerd Wadman, Glenn E Dale
The 1.15A crystal structure of the Staphylococcus aureus methionyl-aminopeptidase and complexes with triazole based inhibitors.
J Mol Biol: 2003, 332(1);13-21
[PubMed:12946343] [WorldCat.org] [DOI] (P p)Alice Douangamath, Glenn E Dale, Allan D'Arcy, Michael Almstetter, Robert Eckl, Annabelle Frutos-Hoener, Bernd Henkel, Katrin Illgen, Sven Nerdinger, Henk Schulz, Aengus Mac Sweeney, Michael Thormann, Andreas Treml, Sabine Pierau, Sjoerd Wadman, Christian Oefner
Crystal structures of Staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate.
J Med Chem: 2004, 47(6);1325-8
[PubMed:14998322] [WorldCat.org] [DOI] (P p)R Y T Kao, K Y Yuen, C M Che, F M Siu
Methionine aminopeptidase as a novel target for antibiotic therapy against Staphylococcus aureus: a proteomic approach.
Hong Kong Med J: 2011, 17 Suppl 2;29-31
[PubMed:21368332] [WorldCat.org] (I p)Sergio C Chai, Wen-Long Wang, De-Rong Ding, Qi-Zhuang Ye
Growth inhibition of Escherichia coli and methicillin-resistant Staphylococcus aureus by targeting cellular methionine aminopeptidase.
Eur J Med Chem: 2011, 46(8);3537-40
[PubMed:21575996] [WorldCat.org] [DOI] (I p)