ID A0A089X3M8_STRGA Unreviewed; 859 AA.
AC A0A089X3M8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 Name=pepN2 {ECO:0000313|EMBL:AIR98417.1};
GN ORFNames=SGLAU_12100 {ECO:0000313|EMBL:AIR98417.1};
OS Streptomyces glaucescens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR98417.1, ECO:0000313|Proteomes:UP000029482};
RN [1] {ECO:0000313|Proteomes:UP000029482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL J. Biotechnol. 194:81-83(2015).
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; CP009438; AIR98417.1; -; Genomic_DNA.
DR RefSeq; WP_043500907.1; NZ_CP009438.1.
DR AlphaFoldDB; A0A089X3M8; -.
DR STRING; 1907.SGLAU_12100; -.
DR MEROPS; M01.009; -.
DR KEGG; sgu:SGLAU_12100; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007335_1_1_11; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000029482; 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; 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:AIR98417.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AIR98417.1};
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:UP000029482};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 107..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 536..845
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 859 AA; 95128 MW; 7A6B6BBFD2E4FEAD CRC64;
MPGTNLTREE AQQRAKLLTV DSYEIDLDLS GAQEGGTYRS VTTVRFDVAE GGAESFIDLV
APAVHEVTLN GDPLDPAEVF RDSRIALPGL LEGRNVLRVA ADCAYTNTGE GLHRFVDPVD
DQAYLYTQFE VPDARRVFAS FEQPDLKATF RFTVRAPEGW TVISNSPTPE PKDNVWEFAP
TPRISTYVTA LIVGPYHSVH SVYEKDGQSV PLGIYCRPSL AEFLDADAIF EVTRQGFDWF
QEKFDYAYPF EKYDQLFVPE FNAGAMENAG AVTIRDQYVF RSKVTDAAYE VRAETILHEL
AHMWFGDLVT MEWWNDLWLN ESFATYTSIA CQAAAPGSRW PHSWTTFANS MKTWAYRQDQ
LPSTHPIMAD IRDLDDVLVN FDGITYAKGA SVLKQLVAYV GEDEFFRGVQ AYFKRHAFGN
TRLSDLLGAL EETSGRDLKA WSKAWLETAG INILRPEIET DADGTVTSFA IRQEAPALPA
GAQGEPVLRP HRIAVGLYDL DETSGKLVRT ERVELDVDGE LTAVPQLAGK RRPAVVLLND
DDLSYAKVRL DEASLRTVTE HLGDFEASLP RALCWASAWD MTRDAELATR DYLSLVLSGI
GKESDIGVVQ SLHRQVKLAI DLYAAPAARE TLLTRWTEAT LAHLRSAAPG SDHQLAWARA
FAATARTPEQ LDLLEALLDG TQTVEGLAVD TELRWAFVQR LAATGRYDEA EIAAEYERDR
TAAGERHAAT ARAARPTPEA KAEAWASVVE SDKLPNAVQE AVIGGFVQTD QRELLAPYTD
RFFEALKGVW ESRSHEMAQQ IAVGLYPSVQ VSQETLDKTD AWLASAEPNA ALRRLVSESR
AGVERALRAQ AADAATAAE
//
