ID   AMPM_KLEOX     STANDARD;      PRT;    43 AA.
AC   P41392;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Methionine aminopeptidase (EC 3.4.11.18) (MAP) (Peptidase M)
DE   (Fragment).
GN   Name=map;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M5a1;
RX   MEDLINE=95272528; PubMed=7753028;
RA   Edwards R.A., Merrick M.J.;
RT   "The role of uridylyltransferase in the control of Klebsiella
RT   pneumoniae nif gene regulation.";
RL   Mol. Gen. Genet. 247:189-198(1995).
CC   -!- FUNCTION: Removes the amino-terminal methionine from nascent
CC       proteins.
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC   -!- COFACTOR: Cobalt; binds 2 ions per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M24A family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X78685; CAA55352.1; -.
DR   PIR; S54755; S43195.
DR   HSSP; P07906; 3MAT.
DR   MEROPS; M24.001; -.
DR   InterPro; IPR002467; Pept_M24A_MAP1.
DR   InterPro; IPR000994; Peptidase_M24.
DR   PROSITE; PS00680; MAP_1; PARTIAL.
KW   Aminopeptidase; Cobalt; Hydrolase.
FT   NON_TER       1      1
FT   METAL        14     14       Cobalt 1 and 2 (By similarity).
SQ   SEQUENCE   43 AA;  4826 MW;  5E030E6D4A3049E1 CRC64;
     TVKTKDRSLS AQYEHTIVVT DNGCEILTLR KDDTIPAIIS HNE
//