ID A0A220SGJ5_9FLAO Unreviewed; 642 AA.
AC A0A220SGJ5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=CEY12_21585 {ECO:0000313|EMBL:ASK32517.1};
OS Chryseobacterium sp. T16E-39.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2015076 {ECO:0000313|EMBL:ASK32517.1, ECO:0000313|Proteomes:UP000198250};
RN [1] {ECO:0000313|EMBL:ASK32517.1, ECO:0000313|Proteomes:UP000198250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T16E-39 {ECO:0000313|EMBL:ASK32517.1,
RC ECO:0000313|Proteomes:UP000198250};
RA Lee S.A., Weon H.-Y.;
RT "Complete genome of Chryseobacterium sp. T16E-39 isolated from tomato
RT (Solanum lycopersicum L.) root endosphere.";
RL Submitted (JUN-2017) 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; CP022282; ASK32517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220SGJ5; -.
DR KEGG; chry:CEY12_21585; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000198250; 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; 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, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..642
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012533088"
FT DOMAIN 54..229
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 309..467
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; 72399 MW; 1D9A5BDCF162EDF4 CRC64;
MKKLYLIVLC IISIGSLHSQ DQNIEMKGLI AKEMKSYAQK MTAPNVNPNT LNYDLQYQRM
DVSLDPAVYN ISGSVTSHFK PNQAMGSIYF DLANSLTVSA VKYHGANLVF QQLPTKEVKI
DFPASLPANV LDSLTIQYAG PPATNNNAFA TGSQNGNLIL STLSEPYGAQ DWFPTKQSLN
DKIDRFDFKI TTPNQYSVAA NGKLMSETTL PNSKKLTFWR TMYPTSAYLI ALAITNFVKL
NDTMGNPPFP FVNYVYPTTQ SNTAVMSNIE WTKQIMNTFE TYFGPYPFRN EKYGHMEFQY
GGVCMEHQTM SSMSSWGRSV IAHELAHQWF GDKVTCGSWN DIWLNEGFAT FGEHLANEKL
LMTQSDFMDY LESQKDYITS SPGGSIYVDD ADLGNQNAIF SGRLSYAKGG YVVRMLKWIL
GDTAFYQAIK EYHSRPNLAY NYAKTADLNA SLLQSTGKNF TEFFNDWIYG EGYPTYDIRW
KESSNQTITI KVAQAQSNSS VSFYEMPLPI KVNGTAGQVA YLKLNNTSNN QYFVESVPFP
IASVQFNYEF QILEKNSTVT KDLTLGVEDL TKDQFSLYPN PAKNELYLKG IERSTDFVIY
AIDGKLVKAG KYQPNKSISI SELVPGVYVF KINDRNIKFV KE
//
