ID A0A2S8WS00_9MICC Unreviewed; 847 AA.
AC A0A2S8WS00;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=pepN {ECO:0000313|EMBL:PQZ93585.1};
GN ORFNames=CQ018_07900 {ECO:0000313|EMBL:PQZ93585.1};
OS Arthrobacter sp. MYb227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1848601 {ECO:0000313|EMBL:PQZ93585.1, ECO:0000313|Proteomes:UP000239972};
RN [1] {ECO:0000313|EMBL:PQZ93585.1, ECO:0000313|Proteomes:UP000239972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb227 {ECO:0000313|EMBL:PQZ93585.1,
RC ECO:0000313|Proteomes:UP000239972};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-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}.
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:PQZ93585.1}.
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DR EMBL; PCPT01000003; PQZ93585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8WS00; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000239972; 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:PQZ93585.1};
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:UP000239972};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 528..837
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 847 AA; 92421 MW; 3566A2CD335620C6 CRC64;
MPGLNLTRSE AQARAEILAV DSYTVELNLT GSDTVFGSKT TVRFNATAGS STFIDAVTSA
VHSVNLNGVE LDPAEVSDGV RIELPNLAAE NILVIDADAL YMNTGEGLHR FVDPVDQEVY
LYSQFEVPDS RRMFAVFEQP DLKAAFTFSV TAPAHWDIIS NSPTPEPVAA HEGAKTWSFA
PTARMSSYIT ALIAGPYKSV RSELTSSDGR IIPLGVFARA SLMEHLDAEN IFTLTRQGFE
FFEAQFGTPY PFEKYDQLFV PEFNAGAMEN AGAVTFLESY VFRSRPTEAM VERRAITILH
ELAHMWFGDL VTMRWWNDLW LNESFAEFMS TLAAAQNTEF TSSWTTFNIL EKTWAYRQDQ
LPSTHPIVAE INDLEDVQVN FDGITYAKGA SVLRQLVAWV GQKEFMAGVR SYFEKHAWGN
TELPDLMREL ETASGRDLSE WTRLWLETAG VNTLRAQIST DDAGLITSFE ITQSAIDAYP
TIRPHRLAVG FYDLDATGAL VRVHREELDI AGASTSVPAL LGLKRPALVL VNDDDLAYAK
IRLDEVSLAT ATEHLKDFDG SLPRTLVWGA AWDAVRDAET PARAYVDLVL NNIGHEKDSS
VIMVLLRQLN TTLDFYVDPA AASAAGTSAA NSLWTLAQDA MAGSDAQLQF VKAFAARAHT
TEQLEIVSTL LDGSLVLAGL QVDADLRWDL LSSLAAGGSA SVADIDDELA HDNTANGSLA
AHSAKAAMPT IEAKAAAWAA IQAGELSNLE QRAAIAGFNR VHDAALIADY VPAYFEAALA
AWETKSYEIA QQIIVGLYPA AQISQETLDT TDTFLAGVGE ESRALRRLIV EARDGVVRSL
AAQAADR
//