ID E0WUG6_9ENTR Unreviewed; 892 AA.
AC E0WUG6;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:EFL91354.1};
GN ORFNames=REG_1747 {ECO:0000313|EMBL:EFL91354.1};
OS Candidatus Regiella insecticola LSR1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX NCBI_TaxID=663321 {ECO:0000313|EMBL:EFL91354.1, ECO:0000313|Proteomes:UP000005726};
RN [1] {ECO:0000313|EMBL:EFL91354.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSR1 {ECO:0000313|EMBL:EFL91354.1};
RX PubMed=19840097;
RA Degnan P.H., Leonardo T.E., Cass B.N., Hurwitz B., Stern D., Gibbs R.A.,
RA Richards S., Moran N.A.;
RT "Dynamics of genome evolution in facultative symbionts of aphids.";
RL Environ. Microbiol. 0:0-0(2009).
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; GL379662; EFL91354.1; -; Genomic_DNA.
DR AlphaFoldDB; E0WUG6; -.
DR STRING; 663321.REG_1747; -.
DR MEROPS; M01.005; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_6; -.
DR Proteomes; UP000005726; Unassembled WGS sequence.
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:EFL91354.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000005726};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 34..202
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 241..454
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 460..560
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 564..884
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 892 AA; 101648 MW; 72D31B9198C833CD CRC64;
MTTSTTQPST IKSEPPVKYR HDYHPPDYTI TDIDLDFTLD AEKTTVTAVS KIKRQIKENA
PLILNGENLV LLSVCVDGQP WKKAYQQNNH LILENLPTNF TLTIVNEIHP ATNTALEGLY
LSNNVLCTQC EAEGFRHITF YLDRPDVLAR FTTRITADKA RYPYLLSNGN CIEKGDCTVK
KGQPDGRHWV KWQDPFPKPC YLFALVAGDF DLLRDHFITR SGRKVSLELF VDRGNLNRAE
WAMTSLKSAM KWDETRFGLE YDLDIYMIVA VDCFNSGAME NKGLNIFNAK YVLANAETAT
DKDYLDIEAV IAHEYFHNWT GNRVTCRDWF QLSLKEGLTV FRDQEFSSDF GSRAVNRIKN
VRLMRSAQFA EDASPMAHPI RPDKVMEMRN FYTLTVYEKG SEVIRMIHAL LGEEKFQAGM
KLYFDRHDGC AVTCDDFVQA MSDASKIDLT LFRRWYSQSG TPLLTIRDSY DAEKQQYHLM
VSQKTLPSRE QAEKLPLHIP LDIELYDDSG NVIALKMNGV AQGSVLNVTK AEQRFTFDQV
NCQPIPSLLR EFSAPVRLDY PYSDQQLTFL MRHARNAFSR WDAAQSLLAI YIKQNVDHAQ
PEAPLSLPPQ VIDAFQTALL DKDLALAAEI VTLPTENEMA EFFTIIDPHA IRRVYYGLTR
CLAKELAEQW QTLYHSNKIT VYSATHGDMA KRALSNICLK YLAFGDNIDV ADQTVSTAYY
QANNMTDALA ALASSVAAQL PCRDELLAHF EQRWQQDGLV MGKWFTLQAT SPADDVLDRV
KNLLKHPSFS LNNPNRTRSL IGSFTASNPA AFHALDGSGY QFLVERLSIL NSKNPQLASR
LIEPLIRFKR YDPERQKLMR NALQQLKTLT NLSSDMYEKI EKALDLFPNR SE
//
