ID   S0EVI7_CHTCT            Unreviewed;       843 AA.
AC   S0EVI7;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=CCALI_02002 {ECO:0000313|EMBL:CCW35809.1};
OS   Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC   Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC   Chthonomonadaceae; Chthonomonas.
OX   NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW35809.1, ECO:0000313|Proteomes:UP000014227};
RN   [1] {ECO:0000313|Proteomes:UP000014227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23976 / ICMP 18418 / T49
RC   {ECO:0000313|Proteomes:UP000014227};
RA   Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA   Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT   "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT   from the Armatimonadetes phylum (formally candidate division OP10).";
RL   Submitted (MAR-2013) 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}.
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DR   EMBL; HF951689; CCW35809.1; -; Genomic_DNA.
DR   RefSeq; WP_016483333.1; NC_021487.1.
DR   AlphaFoldDB; S0EVI7; -.
DR   STRING; 454171.CP488_02087; -.
DR   KEGG; ccz:CCALI_02002; -.
DR   PATRIC; fig|1303518.3.peg.2064; -.
DR   eggNOG; COG0308; Bacteria.
DR   eggNOG; COG1413; Bacteria.
DR   HOGENOM; CLU_014298_0_1_0; -.
DR   InParanoid; S0EVI7; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000014227; 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; 1.25.10.10; 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; PF13646; HEAT_2; 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.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:CCW35809.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCW35809.1};
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:UP000014227};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          57..240
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          274..481
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   843 AA;  93775 MW;  835110F907342861 CRC64;
     MLPHRTRSFI CLLSGLFLVG LSRITAYAQF QRVGGNPFEP PAATLHYARN RDYHVEHLQL
     VFIVHPDTHS AEGTVTHTLA PLRDGLSTIV LDAGANLQIK DCTLDGAPVT FEHNGDKLIL
     HAPSPLQRGK YVKVSVHYIM PSGTVGGGAN GVGGFKWIDP TPSDPHRAPG FWTQGETDTN
     RNWVPCYDYP NDKCTSETIV TVPDTWTVIG NGQEGPVTED KAHHTKTFRW IMNQPHSTYL
     LSLVGGELDV YRTHWGKTPL LYVTPKGQGA LAPYSFSDTP DMLSFYSQLL DFKYPWPKYA
     EDAVYDFPGG MENVSATTLG NIALTDPRAG LVRTDSLTAH ELAHQWFGDT VTCKDWGNIW
     LNEGFATFMQ MLYTRHRFGE EEWQADKEGA LQSYLREANR YLRPLSTKLY SNPDVLFDST
     TYSKGALVLE MLRDQLGQDN LFRGLHHYLE VYKFRPVDSH DLMEAITDET GINVEPFFDQ
     WVYKPGHPVL QMSWHYDPQS ATVQITVKQL QDTSRGVPIF HMPITFGLIY PDRSSSDRLQ
     RVTENCDQAE QEFSIPETAA PAAVLLDPDH ELIKQMETPK WSEAEAKAIL LYAPDYVDRL
     EAARQIVAQP GGLTAEREQL FIQALKSEPA WRVASFLLRQ LGNLKDPALR SLFLQQTESK
     QPERVAAAFE ALSQLPADAA TLNLLHREAI SDTAPYVAVG GALNALAKLA PAQNLDVFRH
     QIEAKTPRDQ LAYIAVNALA EAHVDAAGPL LLEAAGPSHF YFTRLAAIRA LGHLDRSDSS
     VSKGLANLLS DSNPQIQQSV IEALQERGDK SVTPVLQAFE TQTSDPKLKQ AAEDAIANLK
     RGD
//