ID A0A1V9DY66_9BACT Unreviewed; 372 AA.
AC A0A1V9DY66;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peptidase M42 {ECO:0000313|EMBL:OQP38704.1};
GN ORFNames=A4H97_18470 {ECO:0000313|EMBL:OQP38704.1};
OS Niastella yeongjuensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=354355 {ECO:0000313|EMBL:OQP38704.1, ECO:0000313|Proteomes:UP000192610};
RN [1] {ECO:0000313|Proteomes:UP000192610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17621 {ECO:0000313|Proteomes:UP000192610};
RA Chen L., Zhuang W., Wang G.;
RL Submitted (APR-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}.
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:OQP38704.1}.
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DR EMBL; LVXG01000082; OQP38704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9DY66; -.
DR STRING; 354355.SAMN05660816_02708; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000192610; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000192610}.
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 372 AA; 41106 MW; 02224ABD91D59C91 CRC64;
MAKSKTTASA STYTLTDKAF TFLRNYINNP SPVGFESSGQ KLWLNYISPL VDTTFVDPYG
TAVGVINPKA EFKVVIEAHA DEISWFVNYI TPEGLIYLKR NGGVDHVIAP GQRVFIHGKK
GPVKAVFGWP AIHTRLHNPD AKDPSPKVEN LFLDSGARNK KEVEDLGIHI GAVVTYQDGF
DELANDYYIG RAFDNRVGGF MIAEVARLLK ENKKTLPYGL YIVNAVQEEI GLRGAEMIAR
RIKPNVAIIT DVTHDTYTPM INKIIEGDVA CGKGPSLAYG PAVHNKLLSL VQDVAEKNSI
PVQLRTVSRS TGTDTDSFAY ANDGCPSVLI SIPLRYMHTT VEMLHKSDIE QTIRLMYETV
LTLTPKTNLS YL
//