ID A0A2U2ZVU5_9ACTN Unreviewed; 465 AA.
AC A0A2U2ZVU5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=DI272_21100 {ECO:0000313|EMBL:PWI16389.1};
OS Streptomyces sp. Act143.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI16389.1, ECO:0000313|Proteomes:UP000245455};
RN [1] {ECO:0000313|EMBL:PWI16389.1, ECO:0000313|Proteomes:UP000245455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Act143 {ECO:0000313|EMBL:PWI16389.1,
RC ECO:0000313|Proteomes:UP000245455};
RA Valanrebinro G., Kumari S., Rameshkumar N.;
RT "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT of saline tolerant kaipad rice and its draft genome analysis.";
RL Submitted (MAY-2018) 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:PWI16389.1}.
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DR EMBL; QFRX01000001; PWI16389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2ZVU5; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000245455; 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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245455};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..465
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038698467"
FT DOMAIN 57..227
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 312..455
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 465 AA; 50471 MW; 0D78D17BFE214502 CRC64;
MSRSARLVPA CVSVLSALAL TLTACGGGGG VHGTPGGAGV RDPYFPEAGN GGYDVGHYDL
RLSYDPGPHR LSGTARLTAE ATQDLSAFDL DLKGLDVEKV TVEGRAARWN RTGQELTVRP
HDDLDDGETF EVEVRYSGSP LTLTDADGSE EGWLRTAGGA VALGEPIGSM TWFPGNHHPS
DKASYDITVT VPEGLEAVSN GELRGKETRD GRTAFSWHAA EPMAGYLATL AIGDYGIRRS
DAAGVPAYSA VQEGESAKVL ARLPEVMEWA QTNFGPYPFS STGAIIGGED DAEYALETQN
RPFFPGAPDT GLLVHELAHQ WFGDSVTPES WRDMWLNEGF ATYAEWLWEE DEGGDSAQDT
FERLYEDGED EYPDLWAFPP GRPTSAAHIS DDPVYQRGAM VIHKIRQTVG DDTFYDIVQG
WTAAHRHGNA GTDDFTAYVE RQAPDEDFGA IWEEWLYGEG KPARP
//
