ID A0A0Q4DJU5_9MICO Unreviewed; 849 AA.
AC A0A0Q4DJU5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=ASE56_11160 {ECO:0000313|EMBL:KQM36954.1};
OS Microbacterium sp. Leaf203.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1735677 {ECO:0000313|EMBL:KQM36954.1, ECO:0000313|Proteomes:UP000051381};
RN [1] {ECO:0000313|Proteomes:UP000051381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf203 {ECO:0000313|Proteomes:UP000051381};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf203 {ECO:0000313|Proteomes:UP000051381};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQM36954.1}.
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DR EMBL; LMKF01000031; KQM36954.1; -; Genomic_DNA.
DR RefSeq; WP_056231021.1; NZ_LMKF01000031.1.
DR AlphaFoldDB; A0A0Q4DJU5; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000051381; 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:KQM36954.1};
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:UP000051381};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 92..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 528..839
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 849 AA; 93615 MW; 18C865351B921A02 CRC64;
MPGENLTRIE AQERRAIVDT HSYDVQLDLT RGDEVFASRT VVTFAATEGA STFIDLIART
VHAITLNGRS LDPAAVFADS RIALDDLAAE NELVVEADCE YTNTGEGLHR FVDPVDGEVY
LYSQFEVPDS RRMYTVFEQP DLKAAFTFSV TAPARWKVVS NSPTPEPVAV SDDTARWDFP
ATPRISSYIT ALVAGPYEAT YSELTSADGR VIPLGVFARK SLWQYLDADY VFEKTRQGFA
YFEEKFGFPY PFAKYDQLFV PEFNAGAMEN AGAVTFTETY VFRSKVTDAV KERRVVTILH
ELAHMWFGDL VTMKWWNDLW LNESFAEWAS TIATAEATEW EAAWTTFNAM EKTWAYRQDQ
LPSTHPVVAE INDLEDVQVN FDGITYAKGG SVLKQLAAWV GIEQFFAGVA AYFQKHQWSN
TEVGDLLVEL EATSGRDLGD WAKKWLETAG VNTLTPLIEE GADGTITRFA IVQTAPADYP
TIRPHRLGVG FYSVTESGSL ERVHRVEIDV DGDRTEVAEL RGIRRPDLVL LNDDDLAYAK
IRLDERSLAT AIAHLKDISD PLARSLVWGA AWDQTRDAEA SATDYLDLVL QNIGSETEST
TVRTTLGQLQ LAANSYVAPE TRDAARERVA DGLWELAQKA EAGSDSQLQF VTAFASAAST
PAHAETVRAL RDGDTTLEGL EIDTDLSWQL LVSLASAGVV TAADIDEARA ADNTAKGGEF
AAMAKASLPS HAAKQEAWDS LIERADAPNT IVRSTASGFT NPTTVDVLAD FVEPYFAMLL
PIWESRSYQI AQYLIVGLYP AALANKALRD ATRQWLSQNA DAAPALRRLV GENLAGVERA
LAVQERDAQ
//
