ID D9X9G8_STRVT Unreviewed; 862 AA.
AC D9X9G8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=SSQG_02687 {ECO:0000313|EMBL:EFL32169.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL32169.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) 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; GG657757; EFL32169.1; -; Genomic_DNA.
DR RefSeq; WP_003990281.1; NZ_GG657757.1.
DR AlphaFoldDB; D9X9G8; -.
DR STRING; 591159.SSQG_02687; -.
DR MEROPS; M01.009; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007335_1_1_11; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000004184; 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; cd09602; M1_APN; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 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:EFL32169.1};
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:UP000004184};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 114..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..450
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 541..850
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 862 AA; 95899 MW; 3740379C576E36AF CRC64;
MPGTNLTREE AQQRAKLLAV DSYEIELDLS GAQEGGTYRS VTTVRFDVTA EAGAENGAES
FIDLVAPAVH EVTLNGDSLD PAEIFADSRI ALRGLLQGRN ILRVVADCAY TNTGEGLHRF
VDPVDDQAYL YTQFEVPDAR RVFASFEQPD LKATFQFTVK APEGWTVVSN SPTPEPQDNV
WVFEPTPRIS SYITALIVGP YHSVHSVYEK DGQSVPLGIY CRPSLAEYLD SDAIFEVTRQ
GFEWFQEKFD YTYPFKKYDQ LFVPEFNAGA MENAGAVTIR DQYVFRSKVT DAAYEVRAET
ILHELAHMWF GDLVTMEWWN DLWLNESFAT YTSIACQAHA PGSRWPHAWT TFANSMKTWA
YRQDQLPSTH PIMAEIRDLD DVLVNFDGIT YAKGASVLKQ LVAYVGMDEF FRGVQAYFKR
HAYGNTRLSD LLGALEETSG RDLKTWSEKW LQTAGINVLR PEIETDADGV ITSFGIRQEA
PALPAGAKGE PTLRPHRIAV GLYELDDASG KVVRRERVEL DVDGELTAVP QLVGRPRPAV
VLLNDDDLSY AKVRLDEQSL AFVTEHLGDF EWSLPRALCW ASAWDMTRDA ELATRDYLSL
VLSGIGKESD IGVVQSLHRQ VKLAIDLYAD PAAREALLAR WTDATLAHLR AAAPGGDHQL
AWARAFAATA RTPEQLDVLD ALLDGSQTIE GLVVDTELRW SFVQRLAAVG RFDEAEIAGE
YERDRTAAGE RHAATARAAR PTPEAKAEAW ASVVDSDKLP NAVQQAVIGG FVQTDQRELL
APYTDRYFEV VKDIWESRSH EMAQQIAVGL YPTIQVSQET LDKTDAWLSS AEPNAALRRL
VSESRAGVER ALRAQRADAA AE
//
