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Database: UniProt
Entry: A0A0Q4CDF2_9FLAO
LinkDB: A0A0Q4CDF2_9FLAO
Original site: A0A0Q4CDF2_9FLAO 
ID   A0A0Q4CDF2_9FLAO        Unreviewed;       357 AA.
AC   A0A0Q4CDF2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Peptidase M42 {ECO:0000313|EMBL:KQM24485.1};
GN   ORFNames=ASE55_17735 {ECO:0000313|EMBL:KQM24485.1};
OS   Chryseobacterium sp. Leaf201.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1735672 {ECO:0000313|EMBL:KQM24485.1, ECO:0000313|Proteomes:UP000051097};
RN   [1] {ECO:0000313|EMBL:KQM24485.1, ECO:0000313|Proteomes:UP000051097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf201 {ECO:0000313|EMBL:KQM24485.1,
RC   ECO:0000313|Proteomes:UP000051097};
RX   PubMed=26633631; DOI=.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf201 {ECO:0000313|Proteomes:UP000051097};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf201 {ECO:0000313|Proteomes:UP000051097};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KQM24485.1}.
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DR   EMBL; LMKA01000120; KQM24485.1; -; Genomic_DNA.
DR   RefSeq; WP_056222819.1; NZ_LMKA01000120.1.
DR   AlphaFoldDB; A0A0Q4CDF2; -.
DR   STRING; 1735672.ASE55_17735; -.
DR   OrthoDB; 9772053at2; -.
DR   Proteomes; UP000051097; 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   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;  39980 MW;  AE25A6EA5520D4F4 CRC64;
     MKFDKKSLKF LEKYLNTSSP TGYEHEGQKV WMDYIRPYVD AVEVDHYGTC YGIINPEAEF
     KVVIEAHADE ISWYVNYITD DGLIYVIRNG GSDQTIAPSK VVHIHGEKGI VKGVFGWPAI
     HTRGTQNEPV PKIENIFIDC GAVSKQEVEE MGIYVGCMIT YPDEFFEMND RYFVCRALDN
     RIGGFMIAEV ARLLSENKNS IPFGLYITNS VQEEVGLYGA DMIADTIKPN IAIVTDVTHD
     TTTPMIEKKK EGDQKCGDGP VVFFAPSVHH IIRELIIETA KTKNIPFQRA AASRATGTDT
     DAFAHSNGGV PSALISLPLR YMHTTVEIVS KEDVGNVIKL IYETLLSIQP EMKLKYH
//
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