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Database: UniProt
Entry: G8R408_OWEHD
LinkDB: G8R408_OWEHD
Original site: G8R408_OWEHD 
ID   G8R408_OWEHD            Unreviewed;       775 AA.
AC   G8R408;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   OrderedLocusNames=Oweho_1031 {ECO:0000313|EMBL:AEV32040.1};
OS   Owenweeksia hongkongensis (strain DSM 17368 / CIP 108786 / JCM 12287 / NRRL
OS   B-23963 / UST20020801).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Owenweeksiaceae;
OC   Owenweeksia.
OX   NCBI_TaxID=926562 {ECO:0000313|EMBL:AEV32040.1, ECO:0000313|Proteomes:UP000005631};
RN   [1] {ECO:0000313|EMBL:AEV32040.1, ECO:0000313|Proteomes:UP000005631}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 17368 / JCM 12287 / NRRL B-23963
RC   {ECO:0000313|Proteomes:UP000005631};
RX   PubMed=23450211; DOI=10.4056/sigs.3296896;
RA   Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., Del Rio T.G.,
RA   Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA   Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Rohde M., Tindall B.J., Detter J.C., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Genome sequence of the orange-pigmented seawater bacterium Owenweeksia
RT   hongkongensis type strain (UST20020801(T)).";
RL   Stand. Genomic Sci. 7:120-130(2012).
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; CP003156; AEV32040.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8R408; -.
DR   STRING; 926562.Oweho_1031; -.
DR   KEGG; oho:Oweho_1031; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_407031_0_0_10; -.
DR   Proteomes; UP000005631; 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   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   Aminopeptidase {ECO:0000313|EMBL:AEV32040.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005631};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          40..216
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          266..454
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          703..765
FT                   /note="Secretion system C-terminal sorting"
FT                   /evidence="ECO:0000259|Pfam:PF18962"
SQ   SEQUENCE   775 AA;  86106 MW;  42C8A4B9B3F0654D CRC64;
     MWTVLSWSQF SCQEIKSTGI QSAAPSIDYK AKSDTIDILH YSINLDLTEV QQRIIKGYCD
     ITFTPKMSNV NSIRLDLLML PIDSILVDGQ TANYTYNDTI IKLNLGANLS STDTGLIKVY
     YQGSPQGDGS NWGGWHSQSG YYYNLGVGFA ANPHTYGRAW FPCFDNFVEK STYDFTFKTV
     LPLRPYANGI RISETPLSGD TISTFWQMTD QIPTYLTSVA ASNYAEINDT VNAMNGVLPI
     QLMAKPTDSL KLVNSFVNLK PTFHSYESAF GPYEWQKVGY AVTTVGAMEH ATSIHYPVNL
     VNGNLGGEDI MAHELAHHWW GNLVTCETDA DMWINEGMAE FSSHLYAEDV YGREEYLDIV
     QANAFTVLST AHINDDGFKP IQGLDHEYVY GTHVYQKGAM VGHNLRAYLG DNLFFSGLTT
     LLQNNKYGNL NSNQFRDQLA QITGKNLNHF FDNWVFNPGF PQFSIDSMWV YGNSADLTVT
     QRTRQAPSRF VLIPIHITFF SATGDTTSRK MVHTGGKMPT TFTSLPFSPA FALVGYDGFQ
     LSGNTYDEHV INRAGNFAAS QSYMRITANS IQDSAKLIVM HNWAAPGGKI PASKDYRLSP
     QHYWTIQGID LNNADLTGRI TISPAATSLD TELLKNGSDS LVVLYRKDAT EPWELYVNQQ
     KTQISITGYI DLNNLQAGDY TLANSGEKVG LEENDKQHGK IDIYPNPAKD KVFIKFDEAA
     KTYDITMTDA AGKLLYSNEV TSSSHSPLEI SLKNVSTSFV IVSVNGIGSK VSLID
//
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