ID A0A0F5ATD0_9GAMM Unreviewed; 869 AA.
AC A0A0F5ATD0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:KKA45755.1};
GN ORFNames=WN56_01085 {ECO:0000313|EMBL:KKA45755.1};
OS Salinivibrio sp. KP-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Salinivibrio.
OX NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA45755.1, ECO:0000313|Proteomes:UP000033449};
RN [1] {ECO:0000313|EMBL:KKA45755.1, ECO:0000313|Proteomes:UP000033449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KP-1 {ECO:0000313|EMBL:KKA45755.1,
RC ECO:0000313|Proteomes:UP000033449};
RA Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA Kaur N., Bala M., Mayilraj S.;
RT "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT nov., a novel halotolerant gammaproteobacterium isolated from marine
RT sediment and emended description of the genus Salinivibrio.";
RL Submitted (MAR-2015) 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:KKA45755.1}.
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DR EMBL; LAQR01000001; KKA45755.1; -; Genomic_DNA.
DR RefSeq; WP_046073213.1; NZ_LAQR01000001.1.
DR AlphaFoldDB; A0A0F5ATD0; -.
DR MEROPS; M01.005; -.
DR PATRIC; fig|1406902.3.peg.227; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000033449; 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:KKA45755.1};
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:UP000033449};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 226..439
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 444..544
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 548..868
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 869 AA; 98537 MW; 622C98E42D4253D7 CRC64;
MSQQPTAKYR DDYRAPDFTI TDINLEFDLD PNNTLVTAVS QVKRLNDHAT DLVLDGDALT
LVRLDINGDP WTAYSEEAGK LIVRDVPAAF TLTIQTQLDP ENNTALEGLY ISGGAYCTQC
EAEGFRRITY YLDRPDVLAR FTTKVIADKS TYPYLLSNGN KIASGELEGG RHWVEWHDPY
AKPSYLFALV GGDFDVLRDT FVTRSGRDVA LEIFVDKGNL DRADHAMTSL KNAMKWDEER
FDLEYDLDIY MIVAVDFFNM GAMENKGLNI FNSKYVLANA ETATDTDYLG IEAVIGHEYF
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRSVN RISNARIMRG PQFAEDASPM
SHPIRPEKVI EMNNFYTLTV YEKGSEVIRM MHTILGETGF QKGVKLYFER HDGTAATCDD
FVQAMEDASG VDLTQFRRWY SQSGTPVLNV SSTYDPDSKQ LALHVTQHTP PTADQQEKLP
LYIPLDIALY RRDGSVIELQ RHGESVSNVL AVTDAEQTFI FDGVDEQPVL SLLREFSAPV
KLEHDYQDDE LAFLLQHARN DFARWDAGQS LLAKHIKENV ARVQNEQPID VPLSVIDAFR
GVLLSDNTDP ALIAEVINLP TETEVAGWFD IVDVDAIHQV MAAFKQQFAD HMVDEFDAVY
RQYAQPEYQI THKAIGERAL RNACLSYLAH TENGNTHVER HYQAANNMTD TMAALNAANN
AQLPCREPLM KDFSDKWQHD GLVMDKWFML QGANPSETAL EQVKAQMAHP AFTLKNPNRV
RSLVGAFCNR NPARFHAQDG SGYRFLKEIL VTLNQSNPQV ASRLIDPMLK LAYYDHHRQQ
QMRQVLQELA DMDNLAADLY EKVEKTLEQ
//
