ID A0A498BZY9_9MICO Unreviewed; 850 AA.
AC A0A498BZY9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=C7474_1413 {ECO:0000313|EMBL:RLK49274.1};
OS Microbacterium telephonicum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714841 {ECO:0000313|EMBL:RLK49274.1, ECO:0000313|Proteomes:UP000273158};
RN [1] {ECO:0000313|EMBL:RLK49274.1, ECO:0000313|Proteomes:UP000273158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2T63 {ECO:0000313|EMBL:RLK49274.1,
RC ECO:0000313|Proteomes:UP000273158};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:RLK49274.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RCDB01000002; RLK49274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498BZY9; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000273158; 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:RLK49274.1};
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:UP000273158};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 106..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 231..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 527..838
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 850 AA; 92330 MW; 08CBF2F603DEB05C CRC64;
MPGENLTRIE AQERRAIVDT ESYDIALDLT KGAEVFGSRA VIRFRATEGA STFIDLIARE
VREITLNGAP LDPASVFADS RIALAGLAAD NELIVDADCL YTNTGEGLHR FVDPVDGEVY
LYSQFEVPDS RRVFAVFEQP DLKATFRFTV TAPAAWKVVS NSPTPEPLPA GEGTATWSFE
PTPRISSYIT ALVAGPYEAT FSELTSADGR VVPLGVYGRK SLWQHLDADY IFDKTREGFA
YFESKFGVPY PFAKYDQLFV PEFNAGAMEN AGAVTFTETY VFRSKVTDAV KERRVVTILH
ELAHMWFGDL VTMKWWNDLW LNESFAEWAS TIATAEATEW TEAWTTFNAM EKSWAYRQDQ
LPSTHPVVAT INDLEDVQVN FDGITYAKGG SVLKQLAAWV GIEEFFAGVS AYFRKHAWGN
TELSDLLVEL EATSGRDLST WSKKWLETAG VNTLSPELRV DGSGVISRFA IVQTAPADYP
TIRPHRLGVG FYALEGDALV RTHHVEIDVD GDLTEVPKLA GIAQPDLILL NDEDLAYAKI
RLDERSLRTA IAHLGKISDP LGRSLVWGAA WDQTRDAEAS ASDYVDLVLG NIGTETESTT
VRTTLAQLQL AANAYVAPER REATRAKVAD ALWSLATQAD AGSDSQLQFV TGFASAAATP
AQWAQVESLR SGATALDGLE IDADLSWALL VSLAAGGVVT AADIDAALAA DNTAKGGEFA
AQAKAALPDV AAKRVAWASL IDSADLPNTV VRSAAAGFVH PAGIESLSEF VGPYFEMLLP
IWESRTYQIA NYLITGLYPA PLASTALRDA TRGWLEVHAD APAALRRLVA ENLAGVERAL
AVQDADATRG
//
