ID A0A2A8SHX1_9BACI Unreviewed; 357 AA.
AC A0A2A8SHX1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Peptidase M28 {ECO:0000313|EMBL:PEZ09020.1};
GN ORFNames=CN326_04930 {ECO:0000313|EMBL:PEZ09020.1};
OS Bacillus sp. AFS018417.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033491 {ECO:0000313|EMBL:PEZ09020.1, ECO:0000313|Proteomes:UP000220085};
RN [1] {ECO:0000313|EMBL:PEZ09020.1, ECO:0000313|Proteomes:UP000220085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS018417 {ECO:0000313|EMBL:PEZ09020.1,
RC ECO:0000313|Proteomes:UP000220085};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-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:PEZ09020.1}.
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DR EMBL; NTTM01000006; PEZ09020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8SHX1; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000220085; 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:UP000220085}.
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 357 AA; 39348 MW; A1CB2CA257CAF311 CRC64;
MNKETMELFR TLTELQGASG FEHDVRRFMK QELSKYSDEI VQDRLGSIFG LKKGDENGPR
VLVAGHMDEV GFMVTQITKN GMVRFQTLGG WWSQVLLAQR VQIMTDNGPI IGVVGSVPPH
LLSDEQRARP MDIKNMLIDI GADSPEEAHE IGVKPGQQIV PICPFTPMAN PKKIMAKAWD
NRYGCGLAIE LLKELKDEKL PNTLYSGATV QEEVGLRGAQ TAANMIQPDI FYALDAGPAN
DASGDKTQFG QIGKGAVLRL YDRSMVTHRG IREFILDTAE THNIPYQYFV SQGGTDAGRV
HTSNSGVPSA VIGVCARYIH THASILHIDD YAAAKELLIH LVKATDKTTF ETIKQNV
//