ID A0A178KLD5_9GAMM Unreviewed; 869 AA.
AC A0A178KLD5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:OAN17936.1};
GN ORFNames=A3K86_03190 {ECO:0000313|EMBL:OAN17936.1};
OS Photobacterium jeanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=858640 {ECO:0000313|EMBL:OAN17936.1, ECO:0000313|Proteomes:UP000078503};
RN [1] {ECO:0000313|EMBL:OAN17936.1, ECO:0000313|Proteomes:UP000078503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-40508 {ECO:0000313|EMBL:OAN17936.1,
RC ECO:0000313|Proteomes:UP000078503};
RA Li Y.;
RT "Photobacterium proteolyticum sp. nov. a protease producing bacterium
RT isolated from ocean sediments of Laizhou Bay.";
RL Submitted (MAR-2016) 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:OAN17936.1}.
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DR EMBL; LVHF01000012; OAN17936.1; -; Genomic_DNA.
DR RefSeq; WP_068327580.1; NZ_PYMD01000001.1.
DR AlphaFoldDB; A0A178KLD5; -.
DR STRING; 858640.A3K86_03190; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000078503; 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:OAN17936.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000078503};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 89..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 225..439
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 444..545
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 548..867
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
FT COILED 834..869
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 869 AA; 98245 MW; 09B503781FF983EF CRC64;
MAEQPKAKYR ADYKAPEYTI TDIALDFDLQ DTATRVVAVS KVKRLAEQDA ALQLDGDALT
LIRVEVNGES WSDYEETATG LSLTKLPAEF ELTIETEINP EANTLLEGLY KSGGGFCTQC
EAEGFRRITY YLDRPDVLAR FTTKVTADKA SYPYLLSNGN RIAEGELENG RHWVQWQDPF
PKPSYLFALV AGDFDVLRDK FTTCTGRDVE LEIFVDKGNL DRADYAMTSL KNSMKWDEER
FGLEYDLDIY MIVAVDFFNM GAMENKGLNI FNSKFVLANS KTATDTDYQG IEAVIGHEYF
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RINNVRVVRG PQFAEDRGPM
SHPIRPDKVI EMNNFYTLTV YEKGSEVIRM MHTLLGEQNF QAGMKLYFER HDGTAATCDD
FVQAMEDASG IDLTRFRRWY SQAGTPVVSV TTDYDAEQKR YHVTVKQRTA PTAEQEEKQA
LHIPLDIELY DEQGNVIELQ RNGEAVHHVL DVTEEEQVFV FDNVASKPVI SLLREFSAPV
VLEYDYSDEE LVFLMVHARN EFARWDAGQM LLAKYIRDNV TNVQQGKAVE FPASVVDAFR
GALLAEDLDP AFIAEMLTLP SENEIAGWYK QVDVDAINKV VGDIKAILAA EMEDELTAIY
HSLAQPSYTI EHEAMAKRAL RNRCLSYLAC TEQGNALVEA QYQASDNMTD TMAAMAAANS
SELACREAQM KDFSDKWTHD GLVMDKWFAL QGANPAENAL AVVRETMNHP AFDLKNPNRT
RNLVANFCGN NPVRFHAKDG SGYAFLTEIL TALNSSNPQV ASRLIEPFLK YRQYDEARQT
LMRAELEKLA ALENLAKDLF EKVQKALGQ
//
