ID W8VXZ3_9FLAO Unreviewed; 698 AA.
AC W8VXZ3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=NMS_2768 {ECO:0000313|EMBL:BAO56777.1};
OS Nonlabens marinus S1-08.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO56777.1, ECO:0000313|Proteomes:UP000031760};
RN [1] {ECO:0000313|EMBL:BAO56777.1, ECO:0000313|Proteomes:UP000031760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO56777.1,
RC ECO:0000313|Proteomes:UP000031760};
RX PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA DeLong E.F., Kogure K.;
RT "Functional characterization of flavobacteria rhodopsins reveals a unique
RT class of light-driven chloride pump in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
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}.
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DR EMBL; AP014548; BAO56777.1; -; Genomic_DNA.
DR RefSeq; WP_041497287.1; NZ_AP014548.1.
DR AlphaFoldDB; W8VXZ3; -.
DR STRING; 1454201.NMS_2768; -.
DR HOGENOM; CLU_394736_0_0_10; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000031760; 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 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; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:BAO56777.1};
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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..698
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004914254"
FT DOMAIN 34..198
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 236..432
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 698 AA; 79904 MW; BA70531CBD917AE8 CRC64;
MTRLFFIYLT FLSALISSAQ GIDQPSVDFK RAAVDVSFDP SSELVVGSIS FEIDILKATD
QVHIDANNLL EYSVSSTSHP DIKGTTDDAG LLLRARFRES EKATVTITFK SQPNKALYFI
DTDADKRWDQ AWTQGQGKYT SNWLPSIDDM NEKMEWDISI TAPAEFTVIS NGKLISKSTE
SSGIQWNFDM SQPMSSYLVA VVVGDYQVSS QVSSTGIPLD FYYYPQDSSK VASTYQHSRQ
IFDFLEKEIG IGYPWEVYKQ IPVKDFLYAG MENTSATIFS DQFVQDEIGA LDRSYVNVNA
HELAHQWFGD LVTEESGTHH WLQEGFATYY ALLAERALYG DVHYYVNLYE QAELLNDQNQ
SGNTTALMDP NASSLTFYQH GAWAIHALRD LVGDVVFKNS IKVFLKKYAF ENATTDDLLK
IVADQSGKDL TDYKALWLTN KQFPSEEALR LLRKDLFMEA YLQLLARRIS TFDEAYNSYK
ETLKQPVQKE AVLEMVGQLS LHDDARKYKL LEQAAALNNL EIRQLIALTT TEVNDNNKSM
ISSFLTDNSY VTREQSLVLL WNAAGDKKRL LETAKKAWKQ TNESFDLAWL ALAINTEGYT
KTERKKFLQE LQEYTRPSFS TETRQVAFDY LVALDYLDDQ NYLDLYQAAL HHNYRFYEYA
RKLVNEQYAQ EKRRALMDEV VELLTPAEQE KLKLVTDL
//
