ID A0A078KSM6_9GAMM Unreviewed; 860 AA.
AC A0A078KSM6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:CDZ75957.1};
GN ORFNames=BN59_00219 {ECO:0000313|EMBL:CDZ75957.1};
OS Legionella massiliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ75957.1, ECO:0000313|Proteomes:UP000044071};
RN [1] {ECO:0000313|EMBL:CDZ75957.1, ECO:0000313|Proteomes:UP000044071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUN-2014) 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; CCSB01000001; CDZ75957.1; -; Genomic_DNA.
DR RefSeq; WP_043872586.1; NZ_CCVW01000001.1.
DR AlphaFoldDB; A0A078KSM6; -.
DR STRING; 1034943.BN59_00219; -.
DR MEROPS; M01.005; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000044071; 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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:CDZ75957.1};
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:UP000044071};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 80..184
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 224..437
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 442..535
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 539..858
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 860 AA; 98137 MW; B9FFB025F1905355 CRC64;
MPDQTIYRKD YQPPAFSVAT IDLNFDLYDD HALVQNRMLL KRQHEGALHL YGDELELVSL
AMNGKPLDKS SYSMEQDDLI IDNCPEEFSL EVVTRIYPQD NTKLSGLYRS NHLFCTQCEA
EGFRRISYYL DRPDVLAKYS TRITADKAIY PVLLSNGNLT GAGDLADGRH WVQWDDPFKK
PSYLFALVAG DLACVKDKFV TASGKTVDLR IYVEPGNEDK CAHAMTSLQN AMRWDEEVYG
REYDLDIFMI VAVSDFNMGA MENKGLNIFN SKYILARPDT ATDADFAGIE SVVGHEYFHN
WTGNRVTCRD WFQLSLKEGL TVFRDQEFSR DMNSRDVNRI DDVRVLRSAQ FPEDAGSMAH
PVRPESYQEI NNFYTATVYN KGAEVIRMQH TLLGSKGFRR GMDLYFQRHD GQAVTIDDFV
AAMEDANQVD LNQFKRWYSQ AGTPEVEVTS TYVEGTLTLT LTQSCIPTPE CKEKKPFHIP
IRVALFTESG QILPLENNVL QLRDTKERFG FSGLPSKPVV SLLGDFSAPI KLNYQQSEAD
LLALLRFETD GYAKWDAAQR LALSCLTNCF NTERSQWQIP QTLVDAYRHV LQDESLSTAL
RAELLIPPGF EEVAATLDAV DVNAVEQARD FFRAELGKQL YPQMAAMYEL FWQQEDHGMH
AEAYGRRKLR NVCLWFMMKA DEARSLASCQ QQFIKAKTMT DQIASFAALS NCSQKSVQEL
AIDNFYKQWS QDDLVLDKWF SIQATSEAEG TLARVKTLLK HPAFSMKNPN KVRALVGAFC
QANPRHFHAE NGSGYVFLSE ILEIMDQINP QIAARLATPF TRWRRYDSLR QGLMHKELKR
LAELKLSRDL REVVEKSLIV
//
