GenomeNet

Database: UniProt
Entry: B4F2N1
LinkDB: B4F2N1
Original site: B4F2N1 
ID   AMPA_PROMH              Reviewed;         502 AA.
AC   B4F2N1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   19-FEB-2014, entry version 35.
DE   RecName: Full=Probable cytosol aminopeptidase;
DE            EC=3.4.11.1;
DE   AltName: Full=Leucine aminopeptidase;
DE            Short=LAP;
DE            EC=3.4.11.10;
DE   AltName: Full=Leucyl aminopeptidase;
GN   Name=pepA; OrderedLocusNames=PMI3464;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/JB.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master
RT   of both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
CC   -!- FUNCTION: Presumably involved in the processing and regular
CC       turnover of intracellular proteins. Catalyzes the removal of
CC       unsubstituted N-terminal amino acids from various peptides (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC       Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC       including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC       acid amides and methyl esters are also readily hydrolyzed, but
CC       rates on arylamides are exceedingly low.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC       preferentially leucine, but not glutamic or aspartic acids.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
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DR   EMBL; AM942759; CAR46791.1; -; Genomic_DNA.
DR   RefSeq; YP_002153148.1; NC_010554.1.
DR   ProteinModelPortal; B4F2N1; -.
DR   STRING; 529507.PMI3464; -.
DR   MEROPS; M17.003; -.
DR   PRIDE; B4F2N1; -.
DR   EnsemblBacteria; CAR46791; CAR46791; PMI3464.
DR   GeneID; 6801764; -.
DR   KEGG; pmr:PMI3464; -.
DR   PATRIC; 20521660; VBIProMir120933_3392.
DR   eggNOG; COG0260; -.
DR   HOGENOM; HOG000243132; -.
DR   KO; K01255; -.
DR   OMA; ESLMSVM; -.
DR   OrthoDB; EOG6FV8B3; -.
DR   ProtClustDB; PRK00913; -.
DR   BioCyc; PMIR529507:GJIW-3549-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   PANTHER; PTHR11963:SF3; PTHR11963:SF3; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese;
KW   Metal-binding; Protease.
FT   CHAIN         1    502       Probable cytosol aminopeptidase.
FT                                /FTId=PRO_1000098336.
FT   ACT_SITE    281    281       Potential.
FT   ACT_SITE    355    355       Potential.
FT   METAL       269    269       Manganese 2 (By similarity).
FT   METAL       274    274       Manganese 1 (By similarity).
FT   METAL       274    274       Manganese 2 (By similarity).
FT   METAL       292    292       Manganese 2 (By similarity).
FT   METAL       351    351       Manganese 1 (By similarity).
FT   METAL       353    353       Manganese 1 (By similarity).
FT   METAL       353    353       Manganese 2 (By similarity).
SQ   SEQUENCE   502 AA;  54857 MW;  9E4E5738ACC06DF2 CRC64;
     MEFNVKSGSP EKQRSACIIV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKVGQSL
     LLHHVPNVLS ERVLLIGCGK ERELDERQYK QIIQKTINTL NETGSMEAVC FLTELHVKGR
     NNYWKVRQAV ETAKDCLYTF DQLKSNKTEL RRPLRKMVFN VPTRRELPSG ERAIAHGLAI
     ASGIKACKDL ANMPPNICNA AYLASQARQL ADSSANVSTR VIGEEQMKEL NMNAYLAVGQ
     GSQNESLMSI IEYKGNQDPE SRPIVLVGKG LTFDSGGISI KPADGMDEMK YDMCGAATVY
     GVMRVVAELQ LPINVIGVLA GCENMPGGKA YRPGDILTTM SGQTVEVLNT DAEGRLVLCD
     TLTYVERFEP ELVIDIATLT GACMVALGHH YSGLMSNHNP LAHELMNASE QAGDRAWRLP
     LGEEFYEQIE SNFADLANTG GRLGGAITAG CFLARFASKY NWAHLDIAGT AWRSGKAKGA
     TGRPVSLLSQ FLLNRAGLNS DE
//
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