ID B4EVC1_PROMH Unreviewed; 871 AA.
AC B4EVC1;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:CAR41765.1};
GN OrderedLocusNames=PMI0769 {ECO:0000313|EMBL:CAR41765.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR41765.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR41765.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR41765.1,
RC ECO:0000313|Proteomes:UP000008319};
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.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(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}.
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DR EMBL; AM942759; CAR41765.1; -; Genomic_DNA.
DR RefSeq; WP_012367735.1; NC_010554.1.
DR AlphaFoldDB; B4EVC1; -.
DR MEROPS; M01.005; -.
DR EnsemblBacteria; CAR41765; CAR41765; PMI0769.
DR GeneID; 6800827; -.
DR KEGG; pmr:PMI0769; -.
DR PATRIC; fig|529507.6.peg.749; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_6; -.
DR Proteomes; UP000008319; Chromosome.
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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:CAR41765.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAR41765.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 23..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 225..438
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 444..544
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 548..870
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 871 AA; 98869 MW; E97F99CC1201DC86 CRC64;
MTQQRIAKYR KDYRAPDYTI TDLHLDFILD KEKTQVTAIS QCKRLATTVT PLVLDGEDLT
LKSIFVNDVA WTHYKEENGK LIIDQLPEQF TLKIINEINP SANTALEGLY VSGDALCTQC
EAEGFRHITY YLDRPDVLAR YTTTITADKK QYPYLLSNGN RVAQGDLEDG CHWVTWEDPH
PKPSYLFALV AGDFDVLRDT FNTKSGREVA LELFVDKGNL DRADWAMTSL KNAMKWDESR
FNLEYDLDIY MIVAVDFFNM GAMENKGLNV FNSKYVLAKS ETATDKDYLG IESVIGHEYF
HNWTGNRITC RDWFQLSLKE GLTVFRDQEF SSDLGSRSVN RINNVRVMRT AQFAEDASPM
AHPIRPDSVI EMNNFYTLTV YEKGAEVIRM IHTLLGEEKF QAGMQMYIHR HDGSAATCDD
FVQAMEDASN VDLTLFRRWY SQSGTPVLTV RDSYDAQKQQ YTLTVSQMTP PTADQAEKQV
LHIPLDIELY NQQGEVIPLR SQGQPVSNVL NVVREEQQFI FDDVAQQPIP SLLREFSAPV
KLDYPFTDEQ LSFLMKHARN AFSRWDAAQS LLGRYIKENV SRVQKGQPLI LPEMVIDAFR
AVLLDKDIDP ALAALILTLP TDVEAGEAFA IIDPIAIHQA LGFIRKTLAT EMADEFSAVY
HSMHIGAYRV DHGDIAKRDL RNVCLGYLAV ENQQTGNQLV EAQYHNSDNM TDALAALNAA
VMAQLPCKEA LLQEFDDKWH QDGLVMDKWF SLQAMSPATD VLQTVRSLLS HRSFTLANPN
RTRALIGAFV NNNPVAFHAE DGSGYLLLTE ILTDLNSRNP QVASRLIEPF IRLKRYDANR
QEKMRAELLK LKALDNLSGD LYEKITKALA D
//
