ID A0A1S9PCX8_9SPHI Unreviewed; 825 AA.
AC A0A1S9PCX8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=BC343_09130 {ECO:0000313|EMBL:OOQ58800.1};
OS Mucilaginibacter pedocola.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1792845 {ECO:0000313|EMBL:OOQ58800.1, ECO:0000313|Proteomes:UP000189739};
RN [1] {ECO:0000313|EMBL:OOQ58800.1, ECO:0000313|Proteomes:UP000189739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBZ30 {ECO:0000313|EMBL:OOQ58800.1,
RC ECO:0000313|Proteomes:UP000189739};
RA Huang J., Tang J.;
RT "Genomic analysis of zinc-resistant bacterium Mucilaginibacter pedocola
RT TBZ30.";
RL Submitted (JUL-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:OOQ58800.1}.
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DR EMBL; MBTF01000023; OOQ58800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9PCX8; -.
DR STRING; 1792845.BC343_09130; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000189739; 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; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
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 PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000189739};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..825
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013318176"
FT DOMAIN 49..238
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 277..484
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 825 AA; 92627 MW; DE767F49DDE745EE CRC64;
MKIFRAAILA GSIGACALNT AIAQETAPTE TPAYKLYRAT PTKINDLVHT KLDVRFDYAK
RYMYGKEWVT LKPHMYPTDT LRLDAKGMDL KTIAVVKNGK NTPLTFTYDS LSVAIKLDRV
YTAAEKYTIY IDYTAKPNEL HVKGSAAIND AKGLYFINPD GTDKDKPVQI WTQGETEASS
CWFPTIDRPN QKTTEEITMT VPKQYVTLSN GRLVLSKVNK DGTRTDTWKQ ELPHSPYLFM
MAVGDFKVYK DKWRNKEVSY YLEPKYAPYA KDIFGFTPEV IEFYSKILGV DYPWYKYSQI
VVRDYVSGAM ENTSATLHGE YVQGTKRELA DRYYDAGRST IVHELFHQWF GDYVTAESWS
NLTVNESFAD FSESIWAEYK YGKDAGDAHS YEAMQSYLNT PGAKDKNLVR FHYNDKEEVF
DVVTYQKGGR ILYMLRNYLG NAAFYKGLNI YLKTNGLKNG EAQQLRLAME EASGRDLNWF
FNQWYYGAGH PVLNISYKWD EGTKTQTVYL QQTQDGNAFT LPMAIDIYAA GKKTRHQVWM
RDKADTLTFS VPSKPDLVNV DGDKILLTKK TDSKSLDEFA YQYFNAGLFL DRNEAIDYAK
SRQSEKTAQK IIIAAIQDKF YMLRVKAINV ADLTKDDVRN LAVPILVRLA QTDENNLVRA
AAITALGKLK ASGNMNLFKQ SLSSQSYAIQ GAALTAIGLQ NPAEALPLAK SYEKDSEGAL
TQAIINTYAS AGGDAEWPYV SKAISEMGPQ TQFGIMPKFA ALVGRLKNNE YALAGVKTIA
DFGVRFKQYV GPQVAEILGT VKDARAKAGD TASAAAAEKA IADLK
//
