ID A0A1A7R4Z9_9FLAO Unreviewed; 363 AA.
AC A0A1A7R4Z9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative aminopeptidase FrvX {ECO:0000313|EMBL:RAJ26488.1};
GN ORFNames=LX77_00737 {ECO:0000313|EMBL:RAJ26488.1};
OS Gelidibacter algens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gelidibacter.
OX NCBI_TaxID=49280 {ECO:0000313|EMBL:RAJ26488.1, ECO:0000313|Proteomes:UP000248987};
RN [1] {ECO:0000313|EMBL:RAJ26488.1, ECO:0000313|Proteomes:UP000248987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12408 {ECO:0000313|EMBL:RAJ26488.1,
RC ECO:0000313|Proteomes:UP000248987};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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:RAJ26488.1}.
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DR EMBL; QLLQ01000002; RAJ26488.1; -; Genomic_DNA.
DR RefSeq; WP_066430452.1; NZ_QLLQ01000002.1.
DR AlphaFoldDB; A0A1A7R4Z9; -.
DR STRING; 49280.A9996_02405; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000248987; 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:SF20; AMINOPEPTIDASE YSDC-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:RAJ26488.1}; 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 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 363 AA; 40596 MW; F07C196CBB7D3224 CRC64;
MPKKNILDNK SLEFLENYLN NASPTGYEWT GQKLWMDYLT PYVDEFITDT YGTAVGVINP
KAKYKVVIEG HADEISWYVN YIADNGLIYV IRNGGSDHQI APSKIVNIHT KSGIVKGVFG
WPAIHTRDKA KEEAPKPENI TIDVGAKNKE EVEKMGVHVG CVITYPDTFH ILNKDKFVCR
AIDNRIGGFM IAQVARLLHE NKKTLPFGLY ITNSVQEEIG LRGAEMIAER IKPNVAIVTD
VTHDTTTPMI DKKKEGHLEL GLGPVVAYAP AVQQKLRDLI TETAESNKIP FQRSACSRAT
GTDTDAFAYS GMGVASALIS LPLRYMHTTV EMVHRDDVEN VIKLIYESLL NIKENDSFSY
FEN
//
