ID A0A066WT57_9FLAO Unreviewed; 352 AA.
AC A0A066WT57;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Peptidase M42 {ECO:0000313|EMBL:KDN54179.1};
GN ORFNames=FEM21_27240 {ECO:0000313|EMBL:KDN54179.1};
OS Flavobacterium seoulense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1492738 {ECO:0000313|EMBL:KDN54179.1, ECO:0000313|Proteomes:UP000027064};
RN [1] {ECO:0000313|EMBL:KDN54179.1, ECO:0000313|Proteomes:UP000027064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1321 {ECO:0000313|EMBL:KDN54179.1,
RC ECO:0000313|Proteomes:UP000027064};
RA Shin S.-K., Yi H.;
RT "Genome Sequence of Flavobacterium sp. EM1321.";
RL Submitted (MAY-2014) 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:KDN54179.1}.
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DR EMBL; JNCA01000027; KDN54179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066WT57; -.
DR STRING; 1492738.FEM21_27240; -.
DR PATRIC; fig|1492738.3.peg.2710; -.
DR eggNOG; COG1363; Bacteria.
DR Proteomes; UP000027064; 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 CDD; cd05656; M42_Frv; 1.
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 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 352 AA; 39360 MW; 7480850442D33947 CRC64;
MAFLESYLNN ASPTGYESSG QKIWMEYLKP YVDTFITDTY GTAVGVINPD APFKVVIEGH
ADEISWYVNY ITEDGLIYVI RNGGSDHQIA PSKRVNIHTK NGIVKGVFGW PAIHTRNRDK
EENPKISNIF IDLGCETKEQ VEKLGVHVGC VITYPDEFVV LNENKFVCRA IDNRMGGFMI
AEVARLLHEN KVELPFGLYI TNAVQEEVGL RGAEMITQTI KPNVAIITDV CHDSTTPMID
KKIEGETKIG KGPVITYAPA VQNNLRDLII TTAEEKEIPF QRLASSRVTG TDTDAFAYSN
GGVASALISL PLRYMHTTVE MVHKQDVENV IQLIYETLLK IENNETFSYF KS
//