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Entry: A0A2S8WS00_9MICC
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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
//
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