ID B8EN40_METSB Unreviewed; 888 AA.
AC B8EN40;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN OrderedLocusNames=Msil_0194 {ECO:0000313|EMBL:ACK49175.1};
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK49175.1, ECO:0000313|Proteomes:UP000002257};
RN [1] {ECO:0000313|EMBL:ACK49175.1, ECO:0000313|Proteomes:UP000002257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2
RC {ECO:0000313|Proteomes:UP000002257};
RX PubMed=20472789; DOI=10.1128/JB.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(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; CP001280; ACK49175.1; -; Genomic_DNA.
DR RefSeq; WP_012589245.1; NC_011666.1.
DR AlphaFoldDB; B8EN40; -.
DR STRING; 395965.Msil_0194; -.
DR MEROPS; M01.005; -.
DR KEGG; msl:Msil_0194; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_5; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000002257; 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; 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:ACK49175.1};
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:UP000002257};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 25..197
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 236..449
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 455..561
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 566..887
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 888 AA; 96984 MW; 3715A13E470498E9 CRC64;
MRTDSAEPVR LKDYKAPDYL IDSVDLNVKL HPTAARVVSR LSIRPNPNGR PDAALILDGD
GLIVKSIAID RAAPADGVVV VSPQQLALAN PPQRPFTLDV ETEVNPTANS RLMGLFRSGS
AYCTQCEPEG FRRITFFLDR PDVLSVYTVR LEASRAEAPL LLANGNLVEA GELATGEDGV
ARHYAVWHDP FPKPSYLFAL VGGDLGSIHD AFLTRSGRRV ALGIYVEHGK EPLAAYAMDS
LKRAMAWDET AFGREYDLDV FNIVAVSDFN MGAMENKGLN IFNDKYVLAS PATATDADYA
HIEAVIAHEY FHNWTGNRIT CRDWFQLCLK EGLTVFRDHE FSSDMRSRAV HRIADVRALR
AAQFPEDAGP LAHNVRPETY YEINNFYTAT IYEKGAEVIR MLKVLIGAES FSRGMDLYFE
RYDGTAATVE DFISCFAEAS GRDLSDFFRW YRQSGTPLLE AASSYDASAG TFTLHLEQSS
KPTPGQDHKE PFVIPVALGL VGPDGDLPLK TETDNAASAR EIESGVFVLS TPQRTIIFRD
VESRPALSIL RGFSAPVRLD YAASEADLIR LIARDSDSFT RWQAAQTYAS RLLTRAVADI
GAGKSPAEDY DFVDALASVL TESADPAYAA QMITLPSEAD IARDIGENID PDAIHAARFG
LRRAIGKGLS SHLHTVYARL APDGPYSPDA AAAGRRALRN AALDLLCAGE PEEGAALASR
QFASADTMTD EIAALGALAQ TPGETREAAL KTFYRRHAHD ALVVDKWFAL QAMLPDADTL
SRIKDLTGHP AFSFANPNRV RSLVGAFATG NLTRFNAADG SGFDFVVEIV LCLDPKNPQV
AARLLSAFKS WRTLEPGRKA LAEAALRRIA VRDVLSADVR DIVDRSLG
//
