ID A0A151BZZ0_9MICO Unreviewed; 859 AA.
AC A0A151BZZ0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=AZH51_00980 {ECO:0000313|EMBL:KYH45550.1};
OS Branchiibius sp. NY16-3462-2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Branchiibius.
OX NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH45550.1, ECO:0000313|Proteomes:UP000075667};
RN [1] {ECO:0000313|EMBL:KYH45550.1, ECO:0000313|Proteomes:UP000075667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH45550.1};
RA Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT sample.";
RL Submitted (MAR-2016) 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:KYH45550.1}.
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DR EMBL; LVCF01000007; KYH45550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BZZ0; -.
DR STRING; 1807500.AZH51_00980; -.
DR Proteomes; UP000075667; 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; 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:KYH45550.1};
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:UP000075667};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..199
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 242..452
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 538..848
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 859 AA; 94019 MW; 53D304322ACE9A06 CRC64;
MPGTNLTHAE ANARSLLLTV VHYDVHVDVT QGAEFFSTRS TIAFHCSQPG ATTFLDFIGE
SVESVVLNGE SLMPAAVYDG ARIELPQLGV DNVVEVRATG RFMNTGEGLH RFVDPADQEV
YLYTQFEVAD ARRMFAVFEQ PDLKATFAFT ITAPARWEVL SNQPTPEPEP ADGTYVGPGG
SPEPVATWRF EPTPRLASYV TALVAGPYHL VRSSAQTRDG ELALAVGCRK SLAQYLDADN
IFDVTRRGFA YYEDMFDYPY PFAKYDQILV PEFNAGAMEN AGCVTFAEAY VFRGAVTEAI
VEARAQTILH EMAHMWFGDL VTMRWWDDLW LNESFAEWSA TTCAAEATQW SAVWTSFAVA
DKAWAYNQDQ LASTHPIVAE IPDLEAVESN FDGITYAKGA SVLKQLVAYV GRDNFVAGLR
NYFRKHAFGN TVLDDLLTEL EATSGRDLRA WSSLWLQTAG VNTLTPVVTL DDQGRYQEVV
LEQTAPAEHP TLRPQAIAVG LFDLIDNTLH QRLQVRLDVD GPRSIVTDLV GQPQADLLLV
NDEDLGYIKT RLDARSLQTV VANPLALKDS LAQAVVLGAA WDMTRDAAMS GRDFVTMVLA
SITDPMSSMM LRTVLRQMTH TARFFVAPQH RAQVDAQIAD ELRAAAQQAP AGSDAQLQLV
SAFAAAATDP EDVAWLGALL DGSSELPGLA VDTEMRWTLL TGLCSMGAAG DEQIEAELQR
DPSATGHERA ARARASIPTA EAKQAAWDTL INDPTVPNQT INAIALGFST PHDPQLLRPF
VQPYFQELEN IWEARTFAIA QAITSLSFPG SLADQELLDA TNTWLDAHPQ APSGARRAVA
DHRDGLERAL TAQAYDAAH
//
