ID A0A387B7H7_9MICO Unreviewed; 852 AA.
AC A0A387B7H7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:AYF97036.1};
GN ORFNames=D7I47_01395 {ECO:0000313|EMBL:AYF97036.1};
OS Protaetiibacter intestinalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Protaetiibacter.
OX NCBI_TaxID=2419774 {ECO:0000313|EMBL:AYF97036.1, ECO:0000313|Proteomes:UP000278886};
RN [1] {ECO:0000313|Proteomes:UP000278886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2DFWR-13 {ECO:0000313|Proteomes:UP000278886};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 2DFWR-13.";
RL Submitted (SEP-2018) 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; CP032630; AYF97036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387B7H7; -.
DR KEGG; lyd:D7I47_01395; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000278886; 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; 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:AYF97036.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AYF97036.1};
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:UP000278886};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 101..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 531..841
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 852 AA; 93459 MW; 77B5ABE4C92B9F3B CRC64;
MPGENLTRIE AQERKALVEV ESYDVELDLT TGPTTFRSTT TVRFTATPGA STFIDAITAE
VHSVVLNGSE LGAGVADGTR IALDGLAPAN ELVVVADFAY TNTGEGLHRF VDPVDGEVYL
YSQFEVPDSR RVYAVFEQPD LKATFRFTVT APEAWQVVSN SPTPEPERLG DGSAVWHFEP
TPRISSYITA LVAGPYEVVR SELTSSDGRT VPLGVFARKS LFGYLDADYI FDITRKGFAY
FEEKFGYPYP FAKYDQLFVP EFNAGAMENA GAVTFTETYV FRSKVTDAIK ERRVVTILHE
LAHMWFGDLV TMKWWNDLWL NESFAEWAST IATAEATEWT EAWATFQAME KSWAYRQDQL
PSTHPVVADI RDLEDVQVNF DGITYAKGGS VLKQLAAWVG IDAFFAGVGA YFRAHAYGNT
ELADLLRELE AASGRDLSTF SAQWLETSGV NTLKPEIETD AAGVVTGFRV RQTAHPDYPT
LRQHRIAIGF YSFASEAADA PLVRVHRHEF DLAASEWNDV PELVGLPKPD LVLLNDDDLA
YAKIRLDEDS FRVAVAHLAR IEDPLARALV WGSAWDATRD AEIAGRDYVK LVLGNIGPET
ESTTMRLSLT QLTQTARSYV DPATREETIR AVGDGLWALA QGAEPGSDAQ FQFVKFFANV
ASTPEHAAAL AGLRDGSVAL DGLEIDTDLD WELLEGLVLL GEAGELEIAA ALEQDDTANG
QQSAARARAT IPTVEAKEAA LIAALTDAAL PNVVLRNMAL GYTHVNDPAV LAGLTTLYFD
SLTRVWEERN FAIAQYLVQG FYPAPLASRE LVEASNAWLA GNPEVPALRR MVVEGVAGVE
RALAAQERDR QG
//
