ID A0A024H1C3_9MICC Unreviewed; 858 AA.
AC A0A024H1C3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=pepN {ECO:0000313|EMBL:CCQ45823.1};
GN ORFNames=ARTSIC4J27_1778 {ECO:0000313|EMBL:CCQ45823.1};
OS Pseudarthrobacter siccitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=861266 {ECO:0000313|EMBL:CCQ45823.1, ECO:0000313|Proteomes:UP000035722};
RN [1] {ECO:0000313|Proteomes:UP000035722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4J27 {ECO:0000313|Proteomes:UP000035722};
RX PubMed=24948757; DOI=10.1128/genomeA.00526-14;
RA Manzanera M., Santa-Cruz-Calvo L., Vilchez J.I., Garcia-Fontana C.,
RA Silva-Castro G.A., Calvo C., Gonzalez-Lopez J.;
RT "Genome Sequence of Arthrobacter siccitolerans 4J27, a Xeroprotectant-
RT Producing Desiccation-Tolerant Microorganism.";
RL Genome Announc. Announc.2:e00526-e00514(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCQ45823.1}.
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DR EMBL; CAQI01000040; CCQ45823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024H1C3; -.
DR STRING; 861266.ARTSIC4J27_1778; -.
DR MEROPS; M01.009; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000035722; 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; 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:CCQ45823.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCQ45823.1};
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 18..191
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..447
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 529..840
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 858 AA; 93968 MW; 7CB1CD7E2817FDB1 CRC64;
MNLTRAEASG RAELITVESY DVSLDLTRGG KVFGSTTTVK FNARSGSSTF IDAVTASVHS
VTLNGRSLDP ATVSDGVRIQ LPELAEHNEL TVVADVPYMN TGEGLHRFVD PVDNEVYLYT
QFEVPDSRRM FAVFEQPDLK ATFAFTVTAP AHWDVISNSP TPTPVETIPG EDGGARSVWS
FSPTPRLSSY VTALIAGPYQ SVRSEVTSSD GRVIPLGVFA RKSLMQYLDA ENIFELTRQG
FEFFEAQFGC PYPFEKYDQL FVPEFNAGAM ENAGAVTILE GYVFRSKVTG AQVERRAITV
LHELAHMWFG DLVTMRWWND LWLNESFAEY MSHLAAVEAT SFTSAWTTFA SVEKSWAYRQ
DQLPTTHPIF AEINDLQDVE VNFDGITYAK GASVLRQLVA WVGPEQFMAG VREYFAKHSW
QNTELSDLLV ELEKASGRDL DVWGRQWLET AGVNTLKPEL EVDGDGRLTS FAIVQSAVDE
WPTIRPHRLA VGFYNLTGGK LERVHREELD VDGERTEVPA LAGLAQPDLI LVNDDDLAYA
KVRLDEKSLA TATAHLKDFS HSLPRTLVWN SAWDAARDGE TPARRYVELI LANVAAESDS
SVILVQLRQL ATTLNFYVAE EHRQATTVAA ADKLWELAAE VPGGSDAQLQ FVKSFALLAS
SGTQLDQVAG LLDGSFVLDG LAVDQDLRWE LVTSLVAGGR LGQDGIDAEL ARDNTSSGQN
AAAQAKAAIP TPEAKAAAWE SIVVKGELSN ALQGSAVTGF MRVLDRSLLE PYAEKYFQAV
PGIMETRTHA LAQQIVVGLY PSLLTTQSIV DRTDGFLASL PPESAALRRL MLENRDGVAR
ALRARAADVL PGEAVPAA
//
