ID A0A1V1ZJ02_9FLAO Unreviewed; 645 AA.
AC A0A1V1ZJ02;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=BKM32_03460 {ECO:0000313|EMBL:OMP32121.1};
OS Mangrovimonas sp. DI 80.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mangrovimonas.
OX NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP32121.1, ECO:0000313|Proteomes:UP000188854};
RN [1] {ECO:0000313|EMBL:OMP32121.1, ECO:0000313|Proteomes:UP000188854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DI 80 {ECO:0000313|EMBL:OMP32121.1,
RC ECO:0000313|Proteomes:UP000188854};
RA Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT "Taxonomic characterization of strain DI 80 closely related to
RT Mangrovimonas sp.";
RL Submitted (DEC-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 -!- 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:OMP32121.1}.
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DR EMBL; MSDT01000002; OMP32121.1; -; Genomic_DNA.
DR RefSeq; WP_076662547.1; NZ_MSDT01000002.1.
DR AlphaFoldDB; A0A1V1ZJ02; -.
DR Proteomes; UP000188854; 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 Reference proteome {ECO:0000313|Proteomes:UP000188854};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..645
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013138300"
FT DOMAIN 55..233
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 322..469
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 576..640
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
SQ SEQUENCE 645 AA; 72242 MW; DA940EF12886FDD0 CRC64;
MKRFLPLYFF LGSIMCFAQD FDATLKEIST MEAKAALTQL MSVSSVNTGN YDLKYHRLEF
TVDPQVAFIE GEVTTYFEAK ETLTQIYFDL VDDMVVTEVL KNGVSQTFTQ DANDELVITL
SETINAGVLD SLTISYSGNP ENTGLGAFEQ SSHNGDPIIW TLSEPYGAKG WWPCKQDLND
KADSLDVFIT TPKFNPNNEA YIAVANGVEQ SQVMDTETKT THFKHRYPIP AYLVAMAVTN
YEVYNHTVEN NGAPFDIVNY VYPENLDSAQ VNTEVTVDIM ELFTELFEEY PFALEKYGHA
QFGWSGGMEH TTVSFMGSFG RNLIAHELAH QWFGDKITCG SWKDIWLNEG FATYLSGLVI
EDMDEPADFV TWKAQRVNSI TSLPDGAVYL SDADTLSVNR IFSSRLSYNK GAMVLHMLRK
KVGDTDFYQG LTNYLADEDH AYAYAKTVDF IEIMETATGE DLTEFFDDWV YNEGYPTYTL
NCSQPTETTF EIEVNQIQSD PSVSFFEAPV PVRLIGTQGE VLDLVLDNTS DGQVFTELVD
FTVSEVLFDP ESDLISKNDN VTLGVADLAL ASQLRLYPNP TNAVLYIEKP DNVVVEQVDV
YNPLGQLVLK SAETSSIDLT PYSVGMFFVK LTTNKGIINK SVLKN
//
