ID A0A1Q5PDQ3_9BACT Unreviewed; 863 AA.
AC A0A1Q5PDQ3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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};
GN ORFNames=A3841_18870 {ECO:0000313|EMBL:OKL40378.1};
OS Pontibacter flavimaris.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1797110 {ECO:0000313|EMBL:OKL40378.1, ECO:0000313|Proteomes:UP000186551};
RN [1] {ECO:0000313|EMBL:OKL40378.1, ECO:0000313|Proteomes:UP000186551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S10-8 {ECO:0000313|EMBL:OKL40378.1,
RC ECO:0000313|Proteomes:UP000186551};
RA Zhang G., Zhang R.;
RT "Genome sequence of Pontibacter sp. nov., of the family cytophagaceae,
RT isolated from marine sediment of the Yellow Sea, China.";
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:OKL40378.1}.
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DR EMBL; LVWA01000005; OKL40378.1; -; Genomic_DNA.
DR RefSeq; WP_073852481.1; NZ_LVWA01000005.1.
DR AlphaFoldDB; A0A1Q5PDQ3; -.
DR STRING; 1797110.A3841_18870; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000186551; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:OKL40378.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..863
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012818459"
FT DOMAIN 145..218
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 262..468
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 863 AA; 98742 MW; 31FF79332E07FEA1 CRC64;
MKKRNRNLLL ASIALLSAGT LASCSSSAPA TSEAIPVETG VSKELADYRK QVLSHIAYDI
SLQIPEQKQQ PILGEETITF RLSDNSRPMQ LDFKEAPDHL KQVWLNGKQL EVRLENEHIL
LPAKELIVGE NEVRLEFIAG DLSLNRNEEY LYTLLVPDRA RTVLPVFDQP NLKATFKLSL
TLPKDWKALA NGSLVDSAVT ENSKSYTFAT SDTIPTYLFS FAAGKFKHVQ RDMKGTTMHF
YHRETDPAKI RESINPIFQL HSDALRFMEA YTQIPYPFQK FDFVAIPDFQ YGGMEHVGAI
QYKASTLFLD ETATKDEKIS RSNLIAHETA HMWFGDLVTM QWFDDVWMKE VFANFMADKV
TQVALENTNY DMKFLVDHFP AAYSIDRTTG ANPIRQPLDN LQDAGSLYGS IIYHKAPIMM
RQLERLMGEE ELRKGLQEYL KAYAYQNATW PDLINILDAR TPVDLEEWNQ VWVNEPGRPV
FSHELKTSNG KIEQLRVMQQ GEDGSERVWS QFFEIALVYP DRLEELTVDM TNKEVVVGKA
ASKEVPQFIL FNSTGQGYGV FPVEEAMLER LYTLQDPVQR ASAYINLYEN MLNGRNLTPA
QLIRFYQKGL AQEQEELNIK LISGQLSDVY WTFISPAQRR QLAAQLEQEV WQALQQQQAP
NVKKLLFKTY QSIATSKDAQ DRLYQVWQKQ QPPTGVKLNE DDYTSLALAL AVRDYPDQRI
LGEQLTRIQN PDRKKRLEFL MPALSSDAQV RNAFFASLKE AENREKEAWV ASALGYLHHP
LRAQTSADYL PQSLELLAEI QRTGDIFFPF NWLRATFGSY QTAEAAEVVR NFLAANPDYN
PKLKAKILQA ADDLFRAEKL VQE
//