ID A0A1J5L8C8_9BACT Unreviewed; 362 AA.
AC A0A1J5L8C8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peptidase M42 {ECO:0000313|EMBL:OIQ30290.1};
GN ORFNames=BM564_02645 {ECO:0000313|EMBL:OIQ30290.1};
OS Bacteroidetes bacterium MedPE-SWsnd-G2.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1860095 {ECO:0000313|EMBL:OIQ30290.1, ECO:0000313|Proteomes:UP000183188};
RN [1] {ECO:0000313|EMBL:OIQ30290.1, ECO:0000313|Proteomes:UP000183188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE-SWsnd-G2 {ECO:0000313|EMBL:OIQ30290.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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:OIQ30290.1}.
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DR EMBL; MPDE01000002; OIQ30290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5L8C8; -.
DR STRING; 1860095.BM564_02645; -.
DR Proteomes; UP000183188; 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 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 362 AA; 40577 MW; E3B05EBA3DCEFACB CRC64;
MAKKKILNKK SIDFLEKYLN NAAPTGYEWT GQEIWMDYLK PYVDEFITDT YGTAVGVINP
DAKYKVVIEG HADEISWYVN YISDDGLIYV VRNGGSDHQI APSKIVNIHT KKGIVKGVFG
WPAIHTRNKA KEQAPTLENI CIDTGCKTKE EVEKLGVHVG CVITYPDEFH ILNKDIFVCR
ALDNRMGGFM IAEVARLLKE NKKELPFGLY ITNSVQEEIG LRGAEMITHT IKPDVAIVTD
VTHDTTTPMI NKKTQGHCEM GKGPVVAYAP AVQQKLRDLI TDTADKHKIP FQRAALSRAT
GTDTDAFAYS NGGVASALIS LPLRYMHTTV EMVHRDDVEN VIRMIYESLL NIKEGETFSY
FK
//
