ID A0A0C2DJF9_9STAP Unreviewed; 357 AA.
AC A0A0C2DJF9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase M28 {ECO:0000313|EMBL:KIH70123.1};
GN ORFNames=SN16_11585 {ECO:0000313|EMBL:KIH70123.1};
OS Salinicoccus roseus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX NCBI_TaxID=45670 {ECO:0000313|EMBL:KIH70123.1, ECO:0000313|Proteomes:UP000031546};
RN [1] {ECO:0000313|EMBL:KIH70123.1, ECO:0000313|Proteomes:UP000031546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W12 {ECO:0000313|EMBL:KIH70123.1,
RC ECO:0000313|Proteomes:UP000031546};
RA Wang H., Yu B.;
RT "Genome sequences of high lactate-tolerant strain Salinicoccus roseus W12
RT with industrial interest.";
RL Submitted (JAN-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:KIH70123.1}.
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DR EMBL; JXII01000009; KIH70123.1; -; Genomic_DNA.
DR RefSeq; WP_040106761.1; NZ_RKQJ01000001.1.
DR STRING; 45670.SN16_11585; -.
DR GeneID; 77846183; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000031546; 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 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:UP000031546}.
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 322
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; 38824 MW; F59A332D23ED4269 CRC64;
MDKQLQMMKS LTDAHGISGF EYDVKKVMQG YLEPVSDELV QDNLGGIFGK RNAKEGSRTL
LIGGHLDEIG FMVTRIDDEG FIRFTPIGGW WNQVMLSQRM NVVTGSGVLT GVIGSKPPHV
LSQEARKKPV DMKDMFIDIG VASKEEAEEA GVKVGDMITP HCDFTEMANK DYLLAKAWDN
RFGCGVAIEV LESLKDEDVN INVVSGATVQ EEVGLRGAKV AANKVKPDLA IAVDVGISWD
TPGMSEKDGT GKMGDGPLVL LLDGSNIGHV GFRRHVEQLA KDKDIPVQWS AITGGGTDSG
AFHVSNEGVP SISIGVPLRY MHSNVSILNR NDYNNAVRLV TEIVRSLDDS KVEEIIW
//
