ID A0A1K1RYA5_9BACT Unreviewed; 499 AA.
AC A0A1K1RYA5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN05661012_04458 {ECO:0000313|EMBL:SFW77049.1};
OS Chitinophaga sancti.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW77049.1, ECO:0000313|Proteomes:UP000183788};
RN [1] {ECO:0000313|EMBL:SFW77049.1, ECO:0000313|Proteomes:UP000183788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 784 {ECO:0000313|EMBL:SFW77049.1,
RC ECO:0000313|Proteomes:UP000183788};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
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; FPIZ01000015; SFW77049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K1RYA5; -.
DR STRING; 1004.SAMN05661012_04458; -.
DR Proteomes; UP000183788; Unassembled WGS sequence.
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 PANTHER; PTHR11533:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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:0000256|ARBA:ARBA00022438};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 14..177
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..414
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 499 AA; 56828 MW; 723CD76707C09AF6 CRC64;
MFTGIRAQQV DVQSYAISLN LQDTTDQIKA SVSITLKYLQ STRRLKFDLA GMKVKEVFTG
PKKYSFEQDA NALYINVDGK AGEQGIYTIT YGGTPKDGLI ISRNKYGHRT FFTDHWPDRA
HQWFPCIDHP SDKAIFRISV AAPDHYTVVA NGVKKEEVNM GGHMKMTSWE EKVPLATKVM
AFAAADFSVT HSGDVGNIPV DSYVFREDSL HQGYARATQI LPYFIQLVGP FQFEKLANIQ
SKTIFGGMEN AGAIFYAEES PGHEKLESLL AHEIAHQWFG DAVTETDWRH LWLSEGFATY
FTLLYMEHTY STDTLKASLK ADREKIIAFA KRRKTPVVDT TVHSNYMQLL NANSYERGGW
VLHMLRRKIG DERFRAGIRQ YFRDYNGRNA STDDFRAEME RAGGENLKGF FTQWLYTAAI
PELQVNLNYN ESTHTVKMEV IQNQLPLFEF PLEYTLDKTK PLQKLMIKDK VTTVMIPAAA
KPAGIWLDPD INLLAEFAR
//