ID A0A265Q157_9FIRM Unreviewed; 339 AA.
AC A0A265Q157;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:OZV10243.1};
GN ORFNames=CIW83_21335 {ECO:0000313|EMBL:OZV10243.1};
OS Tissierella sp. P1.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC Tissierella.
OX NCBI_TaxID=1280483 {ECO:0000313|EMBL:OZV10243.1, ECO:0000313|Proteomes:UP000216906};
RN [1] {ECO:0000313|EMBL:OZV10243.1, ECO:0000313|Proteomes:UP000216906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:OZV10243.1,
RC ECO:0000313|Proteomes:UP000216906};
RA Bukhtiyarova P.A., Antsiferov D.V., Avakyan M.R., Frank Y.A., Ikkert O.P.,
RA Pimenov N.V., Brasseur G., Tuovinen O.H., Karnachuk O.V.;
RT "Isolation and Characterization of an Anaerobic Sulfidogenic Tissierella
RT from Cu-bearing Coins.";
RL Submitted (AUG-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}.
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:OZV10243.1}.
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DR EMBL; NPMN01000058; OZV10243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A265Q157; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000216906; 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:SF5; ENDOGLUCANASE; 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:OZV10243.1}; 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:UP000216906}.
FT ACT_SITE 198
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 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 339 AA; 37743 MW; 7FA48CA00B4B0106 CRC64;
MLLKQLTELP GVSGNEKEVR DFIISEIKDY VDSFKIDRIG NIIAYKKGKD TNKTLMVTAH
MDEVGLLVKE IDNMGLLKFT TVGGIDKRIL VSKPVLVGKD KIMGVIGAKP IHLQKREEWM
RALSIDELYI DIGAKSKEEA EKLVSIGDYV SFASDYVEFG ESLVKAKALD NRVGCSMLVN
LIKEVKDVSF YAVFTVMEEV GLVGAGPAAY EVNPDISIVL EGTLCYDMPK LDTHLVPTYL
NKGPAISLID RTTVFNHEFR KKIVSIAEKN NIPYQYRKTS MGGNDSGKIH TTKEGSITTT
ISVPCRYIHS PASVMSKNDY GNTYLLLKAI LSEFEREEL
//