ID E8WZV8_GRATM Unreviewed; 887 AA.
AC E8WZV8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=AciX9_0699 {ECO:0000313|EMBL:ADW67769.1};
OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN [1] {ECO:0000313|Proteomes:UP000000343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA Haggblom M.M., Woyke T.;
RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002480; ADW67769.1; -; Genomic_DNA.
DR RefSeq; WP_013579097.1; NC_015064.1.
DR AlphaFoldDB; E8WZV8; -.
DR STRING; 1198114.AciX9_0699; -.
DR PaxDb; 1198114-AciX9_0699; -.
DR KEGG; acm:AciX9_0699; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007335_1_1_0; -.
DR OrthoDB; 9814383at2; -.
DR Proteomes; UP000000343; 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; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
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:ADW67769.1};
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:UP000000343};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..887
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003230502"
FT DOMAIN 108..217
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 257..469
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 558..873
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 887 AA; 98486 MW; 04B8BD600DAED0CF CRC64;
MFAGSPVFRA SRLLLALLAI SSPLAAQSLP EAGISRALAS ARAARLSDLH YKLSYELHPH
AEVTQAHETL TFTDTGTGDL PLDYRDGTLT SASLNGTTIP TQLVNGHIIL PAAALHKDQN
TLTIAFQSNI AAAGKAITRY TDRDDKTEYL YTLFVPMDAS MAFPCFDQPD LKARFTLDIS
APTDWTVIGN TAATSKTARG DSAQSIFPET RPISTYLFAF AAGPFEAIQG NPGEPTIYVR
KSQLTRAKAE APQVQQITAR GVAYLSDYFA QPFPFPKYDL VLIPGFPFGG MEHAGDTFLN
EDGVLFRTAP TASDYFRRDI LVLHETTHQW FGDLVTMRWF DDLWLKEGFA QYMAYKAMAQ
LKPDTNPWKH FYEEIKPLAY AIDETQGTTP IYQNIPNLKD AKSAYGAIVY QKAPAVLKQL
DYFLGDQNFR DGLRLYLKQH AYANAQWADL IGAFQATGKS DVQAWASAWI LQRGMPEVTV
EFSCRGDRLG NIHLMQHDVL ETDAVWPISN QIFLSFPAKP ASAKPFDLPV YEMEPIRVDW
NRPAINVISN HAACPTSIFA NYGDQAYGRF LLDPISEKAV TASLIALSTT PTDPLLKSQL
WGALWDQVHT AQASPRAYAE LALKDLPTEQ DESIARILGG RISAAMHAYL SDKGREALAP
QAESVTADRM IHAPTLGLRI VNYRTFTSIA QTPTALAQIK DLLSGKLTIE GMPLKPLDRW
NLIGTLIQQN DPEAPALLAA EKQRDQSGEG QKYAYAQQAA TPTEATKQQY FADYLRTSSQ
PGGPPAVQED WLTQSLGRFN SWNQTPLTEP YLTRALDALP DIKRNRKIFF LGAWLGSFIG
GQHSPEAQQI FHAWLTRKDI DPDLRLKVLE LSDELDRTVL IRQKFPD
//
