ID A0A220S611_9FLAO Unreviewed; 358 AA.
AC A0A220S611;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Peptidase M42 {ECO:0000313|EMBL:ASK28949.1};
GN ORFNames=CEY12_01975 {ECO:0000313|EMBL:ASK28949.1};
OS Chryseobacterium sp. T16E-39.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2015076 {ECO:0000313|EMBL:ASK28949.1, ECO:0000313|Proteomes:UP000198250};
RN [1] {ECO:0000313|EMBL:ASK28949.1, ECO:0000313|Proteomes:UP000198250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T16E-39 {ECO:0000313|EMBL:ASK28949.1,
RC ECO:0000313|Proteomes:UP000198250};
RA Lee S.A., Weon H.-Y.;
RT "Complete genome of Chryseobacterium sp. T16E-39 isolated from tomato
RT (Solanum lycopersicum L.) root endosphere.";
RL Submitted (JUN-2017) 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; CP022282; ASK28949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220S611; -.
DR KEGG; chry:CEY12_01975; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000198250; Chromosome.
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 214
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 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 358 AA; 40257 MW; C21605D207FA67AF CRC64;
MKFEKKSLKF LEKYLNTSSP TGYEHKGQEV WMDYIRPYVD KIEVDHYGTC YGIINPEAEF
KVVIEAHADE ISWYVNYITD DGLIYVIRNG GSDQTIAPSK VVHIHGENGI VKGVFGWPAI
HTRSANQNEP TPKIENIFID CGATSKKEVE EMGIYVGCMI TYPDEFFEMN NRYFVCRALD
NRIGGFMIAE VARLLKENKK TIPFGLYITN SVQEEVGLYG ADMIADTIKP NIAIVTDVTH
DTTTPMIEKK KEGDQKCGDG PVIFFAPSVH HTIRELIIDT AKTKKIPFQR AAASRATGTD
TDAFAHSNGG VPSALISLPL RYMHTTVEMV SKEDVGNVIS LIYETILKIK PEMKLKYH
//
