ID R4WNQ0_9BURK Unreviewed; 897 AA.
AC R4WNQ0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:BAN22520.1};
GN ORFNames=BRPE64_ACDS07660 {ECO:0000313|EMBL:BAN22520.1};
OS Caballeronia insecticola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN22520.1, ECO:0000313|Proteomes:UP000013966};
RN [1] {ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23833137; DOI=10.1128/genomeA.00441-13;
RA Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT Symbiont of the Bean Bug Riptortus pedestris.";
RL Genome Announc. 1:340-344(2013).
RN [2] {ECO:0000313|EMBL:BAN22520.1, ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RPE64 {ECO:0000313|EMBL:BAN22520.1};
RX PubMed=29863457; DOI=10.1099/ijsem.0.002848;
RA Takeshita K., Tamaki H., Ohbayashi T., Meng X.-Y., Sone T., Mitani Y.,
RA Peeters C., Kikuchi Y., Vandamme P.;
RT "Burkholderia insecticola sp. nov., a gut symbiotic bacterium of the bean
RT bug Riptortus pedestris.";
RL Int. J. Syst. Evol. Microbiol. 68:2370-2374(2018).
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; AP013058; BAN22520.1; -; Genomic_DNA.
DR AlphaFoldDB; R4WNQ0; -.
DR STRING; 758793.BRPE64_ACDS07660; -.
DR MEROPS; M01.005; -.
DR KEGG; buo:BRPE64_ACDS07660; -.
DR PATRIC; fig|758793.3.peg.766; -.
DR HOGENOM; CLU_007993_2_0_4; -.
DR Proteomes; UP000013966; Chromosome 1.
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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:BAN22520.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 103..184
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 224..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 453..561
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 565..896
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 897 AA; 99833 MW; 0FDD2733F084E4C6 CRC64;
MIRRLDYTPP AFLIDSVALE FDLVPARTVV KNTMKLRRNP EAQGDAPRLE LMGEQLEFVS
ATIDGVPHAD VRVNENGLSI GSLPAGAFEL SIESICNPAE NTTLSGLYVS SGNFFTQCEA
EGFRRITYFL DRPDVMATYV VTLRADKAAY PVLLSNGNLI EEGDLPDGRH FARWEDPFKK
PSYLFALVAG KLVCIEERIK SGSGKEKLLQ VWVEPHDLDK TRHAMDSLIH SIRWDEKRFG
LELDLDRFMI VAVSDFNMGA MENKGLNIFN TKYVLANPET ATDTDFSNIE AVVGHEYFHN
WTGNRVTCRD WFQLSLKEGL TVFRDQEFSA DMAAGDVEGA ASAAARATKR IEDVRVLRQM
QFAEDAGPMA HPVRPESYVE INNFYTMTVY EKGSEVVRMY QTLFGRDGFR RGMDLYFKRF
DGQAVTCDDF RHALADANQR DLAQFEGWYS QAGTPRVSVR AKYDAANRRY TLTLTQGYGD
TSDAARDTQK TPLLIPFSVG LIGSNGADLP LRLEGEKEPN GTTRVLEFTE REQSFTFVDV
TEAPLPSLLR NFSAPVIVEY DYTNEELAFL LAHDSDPFNR WEAGQRLATR ELLALAGRAA
KGEALSIDDQ TIAAFARVLD DTTLTPAFRE LALMLPSESY LAEQMSVSDP AAVHAARVFM
SRRLASQLRD KWLAAYEANR TPGGYRPTPE DAGKRGLKNL ALAYLSQLDD PADAVRLAQA
QYDVADNMTD RSAALAALLL ASATNGADPA AADAALADFY RRFENEALVI DKWFALQATQ
RGGPDRKVIE IVRGLMQHPA FTLKNPNRAR SLIFSFCSGN PAQFHAADGS GYAFWAEQVI
ALDALNPQVA ARLARGLELW RRFTPQLREK MHAALSEVAS EAKSRDVREV VEKALAA
//
