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Database: UniProt
Entry: A0A1G9VVP9_9BACI
LinkDB: A0A1G9VVP9_9BACI
Original site: A0A1G9VVP9_9BACI 
ID   A0A1G9VVP9_9BACI        Unreviewed;       362 AA.
AC   A0A1G9VVP9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Putative aminopeptidase FrvX {ECO:0000313|EMBL:SDM75947.1};
GN   ORFNames=SAMN05518871_102177 {ECO:0000313|EMBL:SDM75947.1};
OS   Psychrobacillus sp. OK028.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1884359 {ECO:0000313|EMBL:SDM75947.1, ECO:0000313|Proteomes:UP000198927};
RN   [1] {ECO:0000313|Proteomes:UP000198927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK028 {ECO:0000313|Proteomes:UP000198927};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNHY01000002; SDM75947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9VVP9; -.
DR   STRING; 1884359.SAMN05518871_102177; -.
DR   OrthoDB; 9772053at2; -.
DR   Proteomes; UP000198927; 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:SDM75947.1}; 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        215
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         68
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         216
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         326
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;  39277 MW;  6F34AFD1BB83C069 CRC64;
     MPKLDETLTM LKDLTDAKGI PGNEREPREV MEKYIAPFAD KIEYDNLGSL IAEKVGDANG
     PKIMVAGHLD EVGFMISKID DKGFLSFQTV GGWWSQVMLA QRVTIVTRKG DTITGIIGSK
     PPHILSAEAR KKAADVKDMF IDIGASSKEE AMEWGVLPGD MVVPYFEFSV MNNDKLLLAK
     AWDNRIGCAI AIDVLKALKD EKHPNIVYGV GNVQEEVGLR GAKTTTNKIK PDIGFAVDVG
     VAGDTPGITA KESTSKMGVG PQIVLFDASM VSHKGLRDFV TDTADEHNIP YQFETIPGGG
     TDAGSMHISV NGVPSLAIGV ATRYIHSHAG ILHRDDYENA VKLIVEVIKK LDRDAVNKIT
     FD
//
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