ID A0A3D8YU98_9BACL Unreviewed; 357 AA.
AC A0A3D8YU98;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=M42 family peptidase {ECO:0000313|EMBL:REB06518.1};
GN ORFNames=DVB69_12515 {ECO:0000313|EMBL:REB06518.1};
OS Sporosarcina sp. BI001-red.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=2282866 {ECO:0000313|EMBL:REB06518.1, ECO:0000313|Proteomes:UP000256461};
RN [1] {ECO:0000313|EMBL:REB06518.1, ECO:0000313|Proteomes:UP000256461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI001-red {ECO:0000313|EMBL:REB06518.1,
RC ECO:0000313|Proteomes:UP000256461};
RA Rajandas H., Sivachandran P., Mai C.W., Cheong K.W., Teh C.S.J.,
RA Lim E.S.H., Yap I.K.S., Convey P., Chong C.W.;
RT "Draft Genome of Sporosarcina subantarcticus.";
RL Submitted (JUL-2018) 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:REB06518.1}.
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DR EMBL; QQAK01000013; REB06518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8YU98; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000256461; 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:UP000256461}.
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; 39104 MW; 0145BBDA04B0995A CRC64;
MNNETLAMFK TLTELPGAPG NEHAVRKYLR GELEKYSDEM IQDNLGGIFG VRKGPENSPK
IMVAGHMDEV GFMISGITEN GMLRFQTLGG WWNQVMLAQR VEIITDKGVI PGVIGSIPPH
LLTDEQRAKP MDVKNMLIDI GADDLEDAKR IGIRPGQQAL PVCPFTPMAN PKKIMAKAWD
NRYGCGLALE LLKEVKDVEL PNQLFSGATV MEEVGLRGAQ TAANMIQPDL FFGLDASPAN
DMSGSKTEFG QLGKGTLLRI LDRTMITHRG IREFILDTAE TNNIPYQYFV SQGGTDAGKV
HISNEGVPSA IIGICSRYIH TSSSIIHTDD YAAAKELLVK LVTTCDKTTL ETIKQNV
//