ID A0A1Q3WA80_9BACT Unreviewed; 550 AA.
AC A0A1Q3WA80;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=BGO59_32605 {ECO:0000313|EMBL:OJW70962.1};
OS Spirosoma sp. 48-14.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW70962.1, ECO:0000313|Proteomes:UP000186057};
RN [1] {ECO:0000313|EMBL:OJW70962.1, ECO:0000313|Proteomes:UP000186057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=48-14 {ECO:0000313|EMBL:OJW70962.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJW70962.1}.
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DR EMBL; MKUD01000081; OJW70962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3WA80; -.
DR STRING; 1895854.BGO59_32605; -.
DR Proteomes; UP000186057; 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; 2.60.40.1840; -; 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; IPR038438; PepN_Ig-like_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.
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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..550
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012908215"
FT DOMAIN 40..213
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 257..455
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 550 AA; 61766 MW; 1E610E940EF0B44B CRC64;
MKKNSIEFLI GLLALVATSA CSQSPGYLAR YTQPGVDVQN YAFSLTLSDS TNLIRGETTI
RFTRADDRQT VWFDLIGGKS DTLQTGMTVR SVTLADGKPA PFNQRNDKVF INLPAQPNQA
TELTIRYDGT PKQGLIISRN KFGDRTFFGD NWPNNARNYL PVVDHPSDKA TCSFAVNAPA
TYRVIANGKF MGESSLPNAR KLTRWQENTP IPTKVMVIGA ARFVVDEVGS INGVPVQSWL
YPNDSQKGFV DYRPAKEILQ YFIDRIGPYS YEKLANVEST TIFGGMENAS CIFYNEKIIV
GHKDSDVEAL LAHEIAHQWF GNSATESDWS QLWLSEGFAT YFSALYLEHA YGKDTLNAVL
NQNKGQIFRF SALKPKGTIV DSTASNLMDL LNPNSYQKGG WVLHMLRHEL GDDVFWKGIR
AYYTAYRNRN AQSSDLQAIM EKESGKKLGQ FFQQWLYQPG FPEIVWSSRY DATKKSLVID
VRQAQRTGHL FTIPLTFSLR DNRGRELSRS SKLTLSEQTQ TYTIPAATKP ATVVIDPDNT
VLMRSTQMGN
//
