ID A0A086ADA1_9FLAO Unreviewed; 642 AA.
AC A0A086ADA1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=IW15_04335 {ECO:0000313|EMBL:KFF14665.1};
OS Chryseobacterium soli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=445961 {ECO:0000313|EMBL:KFF14665.1, ECO:0000313|Proteomes:UP000028705};
RN [1] {ECO:0000313|EMBL:KFF14665.1, ECO:0000313|Proteomes:UP000028705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19298 {ECO:0000313|EMBL:KFF14665.1,
RC ECO:0000313|Proteomes:UP000028705};
RA Stropko S.J., Pipes S.E., Newman J.;
RT "Genome of Chryseobacterium soli DSM 19298.";
RL Submitted (JUL-2014) 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:KFF14665.1}.
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DR EMBL; JPRH01000001; KFF14665.1; -; Genomic_DNA.
DR RefSeq; WP_034709478.1; NZ_JPRH01000001.1.
DR AlphaFoldDB; A0A086ADA1; -.
DR STRING; 445961.IW15_04335; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000028705; 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; cd09603; M1_APN_like; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR Pfam; PF18962; Por_Secre_tail; 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 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 Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 55..231
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 313..468
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 577..640
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
SQ SEQUENCE 642 AA; 72643 MW; 6852AE1A79035BE0 CRC64;
MRNFYIVLIS FIFGQQLYAQ NLNQNIEMKG LIVKEMKSYT HKMTTYNLNP NTLNYDLMYQ
RLEVSLDPAV YNISGSVTSH FKPNQSMGSM YFDLDNTLMV SQIQYHGSNL LFQHLATKEV
KVDFPVALPA NTLDSLTIFY SGAPATTNNA FSIGTQSSTA ILSTLSEPYG AQDWFPTKQS
LNDKIERFDF KITTPSQYSV AANGKFMSET LLPNAQKLTF WRTAYPTSAY LIGLSITNFT
KITDTMGTPP FPFVNYVYPS TAANTTSMSN IEWTKQVMNL FETYFGPYPF RNEKYGHMES
KYGGGMEHQT MSSMGSWSKN LIAHELTHQW FGDKVTCGAW NDIWLNEGFA TFGTHLANEK
LIMSNTEFMN YLLGQKDLIT SSPGGSTYVS DTNLANVNAV FDSRLSYAKG AYILRMLKWM
LGDTVFFQAL REYHARPALA YNYVRTADFN ASLLQSTGKD FTGFFSDWLY GEGYPTYTIR
WKQSGNQIII KASQAQSNPS VSFFEMPLPI KVNGTGGQAA YFALDNTSDN EYFSESVSFP
IASVEFNYEY QILEKNSTVI QDTSLSTESA AFENFALYPN PAKNEIYVKG IHKEADYSIH
TIDGRLVKKD TYQPHKPVVI SELIPGTYIF TIKDQNIKFI KH
//
