ID M2ZWW1_STRMB Unreviewed; 838 AA.
AC M2ZWW1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=H340_27639 {ECO:0000313|EMBL:EME97208.1};
OS Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME97208.1, ECO:0000313|Proteomes:UP000011740};
RN [1] {ECO:0000313|EMBL:EME97208.1, ECO:0000313|Proteomes:UP000011740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EME97208.1,
RC ECO:0000313|Proteomes:UP000011740};
RX PubMed=23558536;
RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT Transglutaminase.";
RL Genome Announc. 1:E0014313-E0014313(2013).
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:EME97208.1}.
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DR EMBL; AORZ01000136; EME97208.1; -; Genomic_DNA.
DR AlphaFoldDB; M2ZWW1; -.
DR STRING; 1223523.H340_27639; -.
DR MEROPS; M01.012; -.
DR PATRIC; fig|1223523.3.peg.5611; -.
DR eggNOG; COG0308; Bacteria.
DR Proteomes; UP000011740; 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; 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 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:EME97208.1};
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 230..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 520..830
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 838 AA; 92651 MW; FBA53C97E5B131B6 CRC64;
MAPMTVLTRD EAQARARLLD VHSYDIDLDL TRGEEQFRST TVIRFHARTP GDTFVEVRPA
ALLSATLDGR PLDITSLDDN RLPLAALTPG DHELRVEADM RYSRTGEGMH RFTDPVDGET
YLYTQLFLDD VQRVFAAFDQ PDLKAVFSAT VTAPPAWTVL GNTVATRVGP PAEGRWKLPP
GRPLSTYFVA FAAGPWHTVR TEHAGLPFAL HCRRSLAPHL DADADELLGL TRRCFDRFHQ
IFDEPYPFDS YDQAFVPEYN FGAMENPGLV VLRDEYVFRS AATDTERQTR AVTIAHEMAH
MWFGDLVTLR WWDDIWLNES FAEYMGYQVL TDATHVTGPW TEFGVSRKAW GYAADQRETT
HPVAPEPGAV HDTAAALLNF DGISYAKGAS ALRQLVAWLG EKDFLAGINT HFARHRFGNA
TLADFLDSLA GATERDVHAW ADRWLRTTGV DTLTPRITTT DSGWELTVDH EGTRPHRIAV
GLYDHDPDDP GRLTARTREE IDLPGPTGPA LTGTGPRPAL VLLNDGDLAY AKIRLDPDSH
DTALGALSGL PDPLTRAVLW NSLRDQVRDG LLPSDAYLRA TRDHLPHETD NAVVEGVLTF
ARDQIADVYL PADHRDDALA ILRDTCHDLL RRTGQGTAPG PRLAAVRTLI DSATTDAALH
DWLRAGTVPG GPALDPELRW RVLTRLAVLG AVTPDAIAAE LAADPSATGR EGAARCRAAL
PDPAAKQAAW HSLYADDSLS AYLWTATAQG FWQAEQLDLT RPYRDRYHPD ATALAARRGT
ALAKAAGNHG FPRPHIDHDT LRLGEECLSG TEPTPAFRRQ LRDRLDDLRR ALAVRYTQ
//
