ID B0SRI7_LEPBP Unreviewed; 880 AA.
AC B0SRI7;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN Name=pepN2 {ECO:0000313|EMBL:ABZ99479.1};
GN OrderedLocusNames=LEPBI_I3417 {ECO:0000313|EMBL:ABZ99479.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ99479.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ99479.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 {ECO:0000313|EMBL:ABZ99479.1};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000786; ABZ99479.1; -; Genomic_DNA.
DR RefSeq; WP_012390335.1; NC_010602.1.
DR AlphaFoldDB; B0SRI7; -.
DR STRING; 456481.LEPBI_I3417; -.
DR MEROPS; M01.009; -.
DR KEGG; lbi:LEPBI_I3417; -.
DR HOGENOM; CLU_007335_1_1_12; -.
DR OrthoDB; 100605at2; -.
DR BioCyc; LBIF456481:LEPBI_RS16740-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09602; M1_APN; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ABZ99479.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABZ99479.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 44..213
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 255..464
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 545..863
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 880 AA; 102665 MW; 91AD42ABDF312030 CRC64;
MKQTLAILII GFLLIFQHCR LTKPNYHLTL QEAEYRYETI ENIKYNLDIQ LSTKDSFTGK
VDIQFVGKRI RDLRLDYFQG EIKSIVFNDE PLTQFEYKNG QVQLPSDRMM IGNNSLSIRF
ETPFAKTGNG LHKFLDPDDK ETYIYSQFEA FHANKMFPCF DQPDLKATFQ LSVTAPKNWK
VISTTLPTSE TKTENPEEVL HQFPESKKIS TYVFSLHAGP YQVWEDSYES IPLRLFVRKS
LAKYIDPKDW FLFTKDGFAF FNSYFGIPYP FQKYDQIIVP EFNFGAMENV AAVTFSERFV
SRSPMTRNQR ENLSDVILHE MAHMWFGNLV TMKWWNGLWL NESFATYMAS LAQAKNSEFQ
ETWISFFEKM KQWAYEEDSF STNHPVEAKV NDTEEAFTQF DGITYGKGAS VLKQLVFFIG
EESFQKGVQN YLRKYSYSNS TLVDFLKELE FASGFSMKKW SKDWLETKGT NQIELTTICA
DNHLYGKIVQ SAPGPENKLR DHKTVLGLYF FDRSNKQISY EEFPVVYSGR SSQAILQVKS
CPDYVFINAE DHDFAIWSWT SVNKDNLEFV LEFDNDPMRK LILWTDYFRQ VSLANLSFDE
FKETAIRLYP METDTKIKRW LLSRLTSDTG SSYFTSRFWF PESKRNNHLD SLQNFILSEL
TKAKAGSDEQ KYLFLSLIDS SFTESSQKRL YEILENKLSF PGLKLDQDLR WNMIVKLSSL
AIDRNKIQTM IDREKKLDPS NRGVNSSLAA EAAEPNPKIK DKWIQILLNP KASDYSSSTL
RVVSYSLFPE HQKGIQLQFL DTYFAALDKF QHTDDENYLD AFAKSLAPDF CTDETLLILK
KFTNNHPKLP ASVKKTLWKQ IDSEKRCIQI KNKHKDLILE
//
