ID A0A132NDN7_HYDSH Unreviewed; 353 AA.
AC A0A132NDN7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 03-MAY-2023, entry version 25.
DE SubName: Full=Peptidase M28 {ECO:0000313|EMBL:OAR05046.1};
GN ORFNames=SA87_05785 {ECO:0000313|EMBL:OAR05046.1};
OS Hydrogenibacillus schlegelii (Bacillus schlegelii).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family X. Incertae Sedis; Hydrogenibacillus.
OX NCBI_TaxID=1484 {ECO:0000313|EMBL:OAR05046.1, ECO:0000313|Proteomes:UP000243024};
RN [1] {ECO:0000313|EMBL:OAR05046.1, ECO:0000313|Proteomes:UP000243024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA 48 {ECO:0000313|EMBL:OAR05046.1,
RC ECO:0000313|Proteomes:UP000243024};
RA Hemp J.;
RT "Draft genome sequence of Hydrogenibacillus schlegelii DSM 2000.";
RL Submitted (SEP-2015) 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:OAR05046.1}.
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DR EMBL; JXBB01000006; OAR05046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132NDN7; -.
DR STRING; 1484.SA87_05785; -.
DR Proteomes; UP000243024; 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:UP000243024}.
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 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 353 AA; 37493 MW; 99C2A9E4F4188789 CRC64;
MPYDEALFRQ LIEAPGAPGF EGEVRRVVEA ALAGAADRMI RDRLGSLFGV LDGPEGGPTV
MVAGHLDEVA LMVTEVTDDG LLKVTALGGI YEPVLLAQRV FVLGRNGAVP GVIGAPPPHG
LSEEARREAP QLERMFVDVG AASREDVRAF GIRPGDPVVF PGVYTPSWSG RRVLAKAWDN
RFGVGLAVEL LRALRDRPRV NTVVAGATVQ EEVGLRGAET AARLVRPDVF FALDAGPAGD
MPGGSGLGRL GGGVLMRVMD RTMVTHRRLL DYLLDLAEAE GIPYQFFVSR GGTDAGRVHT
MGIGVPSAVI GIPARYIHGP VAIIDLDDYR AAKRLLIAAV SRLDRATLEA IVG
//