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Database: UniProt
Entry: A0A1I0Q0S4_9FLAO
LinkDB: A0A1I0Q0S4_9FLAO
Original site: A0A1I0Q0S4_9FLAO 
ID   A0A1I0Q0S4_9FLAO        Unreviewed;       357 AA.
AC   A0A1I0Q0S4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Putative aminopeptidase FrvX {ECO:0000313|EMBL:SEW20462.1};
GN   ORFNames=SAMN05421841_1573 {ECO:0000313|EMBL:SEW20462.1};
OS   Chryseobacterium wanjuense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=356305 {ECO:0000313|EMBL:SEW20462.1, ECO:0000313|Proteomes:UP000199469};
RN   [1] {ECO:0000313|EMBL:SEW20462.1, ECO:0000313|Proteomes:UP000199469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17724 {ECO:0000313|EMBL:SEW20462.1,
RC   ECO:0000313|Proteomes:UP000199469};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000256|PIRSR:PIRSR001123-2};
CC   -!- SIMILARITY: Belongs to the peptidase M42 family.
CC       {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR   EMBL; FOIU01000001; SEW20462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0Q0S4; -.
DR   STRING; 356305.SAMN05421841_1573; -.
DR   OrthoDB; 9772053at2; -.
DR   Proteomes; UP000199469; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008007; Peptidase_M42.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR   Pfam; PF05343; Peptidase_M42; 1.
DR   PIRSF; PIRSF001123; PepA_GA; 1.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:SEW20462.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   357 AA;  40155 MW;  7E77D1EF447EF9AD CRC64;
     MKFEKKSLKF LEKYLNTSSP TGYEQEGQKI WMDYIRPYVD KIEVDHYGTC YGIINPDAEF
     KVVIEAHADE ISWYVNYITD DGLIYVIRNG GSDQLIAPSK VVHIHGENGI VKGVFGWPAI
     HTRANQNEPI PKIENIFIDC GATTKKEVEE MGIYVGCMIT YPDEFFEMND RYFVCRALDN
     RIGGFMIAEV ARLLKENKKT IPFGLYITNS VQEEVGLYGA DMIADTIKPN IAIVTDVTHD
     TTTPMIEKKK EGDQKCGAGP VVFFAPSVHH TIRELIIDTA KAKKIPYQRA AASRATGTDT
     DAFAHSNGGV PSALISLPLR YMHTTVEMVS KEDVGNVIKL IYETVLKIKP EMKLKYH
//
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