ID A0A1G6K4E3_9BACI Unreviewed; 355 AA.
AC A0A1G6K4E3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Aminopeptidase FrvX {ECO:0000313|EMBL:SDC25870.1};
GN ORFNames=SAMN05421737_106193 {ECO:0000313|EMBL:SDC25870.1};
OS Shouchella lonarensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1464122 {ECO:0000313|EMBL:SDC25870.1, ECO:0000313|Proteomes:UP000242662};
RN [1] {ECO:0000313|Proteomes:UP000242662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25nlg {ECO:0000313|Proteomes:UP000242662};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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}.
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DR EMBL; FMYM01000006; SDC25870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6K4E3; -.
DR Proteomes; UP000242662; 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:SF21; 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:SDC25870.1}; 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:UP000242662}.
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 355 AA; 38169 MW; 2265FCD1FCF21B36 CRC64;
MDERLKMLKA LTDANGISGF EQEARDVMKS YIAPYADEVT TDQLGSLVAK KVGAEDGPKI
MVAGHLDEIG FMVTKIDDKG FIRFQTIGGW WGQVMLAQRV TVMTKAGNID GVIGSTPPHV
LSPEARKKPV DIKDMFIDIG ASSKEEATEF GVKPGDPIVP VCEFTVMKND KLLMAKAWDN
RVGCAIAIDV LRELKDVAHP NTVYGVGTVQ EEVGLRGAKT SAHMIKPDIA FGVDVGIGAD
TPGAKGEGKL GDGPQIILYD ASMIAHKGLR DLVVQVADEQ KIPYQYDAIS GGGTDSGAIH
LTADGVPALS ITVATRYIHT HAGIMHRDDY ENAVKLIVEV IKKLDNDTVK ALTFQ
//
