ID A0A1X6X708_9MICO Unreviewed; 851 AA.
AC A0A1X6X708;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=FM110_12105 {ECO:0000313|EMBL:SLM95041.1};
OS Brachybacterium nesterenkovii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM95041.1, ECO:0000313|Proteomes:UP000195981};
RN [1] {ECO:0000313|EMBL:SLM95041.1, ECO:0000313|Proteomes:UP000195981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP104813 {ECO:0000313|EMBL:SLM95041.1,
RC ECO:0000313|Proteomes:UP000195981};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FWFG01000107; SLM95041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6X708; -.
DR Proteomes; UP000195981; 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:SLM95041.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SLM95041.1};
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:UP000195981};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 96..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 236..442
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 531..840
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 851 AA; 93938 MW; 8FF0EF22431E6E7C CRC64;
MPETQNLTRE EARERASFLS TTDYEVRLDL TGSPTTFRTE STIRFTSSEA RPTFVDLLAP
AVHEIELNGE LLDDPASRFD GARVSLPALR EGDNVVRILA DGAYMNTGEG LHRFVDPVDD
EVYLYTQFEV SDARRMFACF EQPDLKATFA FTITAPAHWR VISNSPTPEP TAIGDGVATW
EFEPTERIST YLTALIAGDY RGGEGSVTLR DGREVPMGVY CRASLVEHLD PDNVIDVTAQ
GIAFYEDAFD CAFPFPKYDQ VFVPEYNMGA MENPGAITYV EKYVFRSEVS DAIRERRDLT
ILHELAHMWF GDLVTMRWWD DLWLNESFAE YASTLCMAEA TRWKDAWTTF AGSEKAWAYN
QDQLPSTHPI VADMVDLDAV ETNFDGITYA KGASVLRQLV AYVGEDAFFE GLRAYFRKHA
WSNTELTDLL VELEATSGRD LAPWSALWLE RAGVTTLCPV IERDADGAVT AFAIAQTAPA
EHPVLRPHRL RVGGYSLQDD GRLVQTEGYE IDVDGERTEV PQAIGGRADL WLVNDGDLAY
AKIRLDDASL AIAMEHLRDI DDPLARTLIW GAAWDMVRDG ELASRRFHEL VLANITGEHQ
SSVIRTLLGQ LGAVTGRFAA PADRDARTAA TADALWELAR GAEAGSDAQL QFVEAFALHA
CTAEHAATLS GLLDGSVTLP GRRIDTDLRW SLVISLASLG GIDAEGIDAV LADDDTASGR
QRALTARAAL PTPEAKQEAW EKTVGSDTLA NESVTAVVQG FWRVHDEALV APYVEPYFAM
LDDVWASRSS EIANRLIQGY FPSDAPTPRI VAAADQWLVD HIDAPLGLRR PIIEGRDSAA
RALRVQEADR A
//
