ID C9Z0M9_STRSW Unreviewed; 493 AA.
AC C9Z0M9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN OrderedLocusNames=SCAB_24731 {ECO:0000313|EMBL:CBG69582.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69582.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG69582.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG69582.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG69582.1; -; Genomic_DNA.
DR RefSeq; WP_013000273.1; NC_013929.1.
DR AlphaFoldDB; C9Z0M9; -.
DR STRING; 680198.SCAB_24731; -.
DR GeneID; 24306236; -.
DR KEGG; scb:SCAB_24731; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_014298_2_0_11; -.
DR Proteomes; UP000001444; 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 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:UP000001444};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..493
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039484780"
FT DOMAIN 162..222
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 263..467
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 493 AA; 53978 MW; D794C031702049AB CRC64;
MPLTPRSGSR RVQAALLASA VSVCLIAASA PSPAVPLGVG DRLFPHLGNP GYDVRSYDLT
LSYPGGNREP LTAVTTIDAR TTSRLERINL DFSHGKVGSV DVDGEPAAFT SAGEDLVITP
REPLSEGSRT RITVRHTSDP VYPQGVEGGW LQTADGLAMA NQADAAHVVF PCNDHPSDKA
MFTVRVTVPD GYTAVSNGLA TRTDRAAGTT TWTYRTQHPM ATELAQVSIG RSAVVRRMGP
HGLPVRDVVP AKDREKLEPW LAKTPAQIEW MEDKVGPYPF ETYGVLIAEA QTGFELETQT
LSLFERELFV RPEYPRWYVE SIMVHELAHQ WFGNSVSPRT WSDLWLNEGH ATWYEALYAE
EVAGRTLEAR MKAAYGASDR WRAAGGPPAA PKAPKDGQKI GIFRANVYDG AALFLYALRQ
EIGAPAFDRL QRAWVTVHRD GVASTSDFRD LASVIAGRDL GAFFHAWLYE LRTPPMPGHP
DWKPVPAAAP AKR
//
