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Database: UniProt
Entry: A0A133Q630_STALU
LinkDB: A0A133Q630_STALU
Original site: A0A133Q630_STALU 
ID   A0A133Q630_STALU        Unreviewed;       358 AA.
AC   A0A133Q630;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=M42 family peptidase {ECO:0000313|EMBL:TBW73525.1};
DE   SubName: Full=M42 glutamyl aminopeptidase {ECO:0000313|EMBL:KXA38337.1};
GN   ORFNames=EQ812_01605 {ECO:0000313|EMBL:TBW73525.1}, HMPREF3225_01293
GN   {ECO:0000313|EMBL:KXA38337.1};
OS   Staphylococcus lugdunensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=28035 {ECO:0000313|EMBL:KXA38337.1, ECO:0000313|Proteomes:UP000070063};
RN   [1] {ECO:0000313|EMBL:KXA38337.1, ECO:0000313|Proteomes:UP000070063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJR7738 {ECO:0000313|EMBL:KXA38337.1,
RC   ECO:0000313|Proteomes:UP000070063};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TBW73525.1, ECO:0000313|Proteomes:UP000293637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E7 {ECO:0000313|EMBL:TBW73525.1,
RC   ECO:0000313|Proteomes:UP000293637};
RA   Williams M.R.;
RT   "Quorum sensing between bacterial species on the skin protects against
RT   epidermal injury in atopic dermatitis.";
RL   Sci. Transl. Med. 0:0-0(2019).
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:KXA38337.1}.
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DR   EMBL; LRQI01000052; KXA38337.1; -; Genomic_DNA.
DR   EMBL; SCHB01000001; TBW73525.1; -; Genomic_DNA.
DR   RefSeq; WP_002478655.1; NZ_SCHB01000001.1.
DR   AlphaFoldDB; A0A133Q630; -.
DR   STRING; 28035.B6N84_02380; -.
DR   GeneID; 58091231; -.
DR   PATRIC; fig|28035.7.peg.1309; -.
DR   eggNOG; COG1363; Bacteria.
DR   OMA; MVSHKGL; -.
DR   Proteomes; UP000070063; Unassembled WGS sequence.
DR   Proteomes; UP000293637; 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:KXA38337.1}; 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        212
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         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         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   358 AA;  39230 MW;  2DA87CEDD000CE90 CRC64;
     MKASIELLKT LTDVNGIAGQ EMQVKETMRD YLNPISDSII EDHLGGIFGK REATYGTKSI
     MLAGHLDEIG FIVTKIDNEG FIKFQPIGGW WSQVMLSQKV TITTDQGQEI RGIIGSKPPH
     VLEAEERKKA VDIKDMFIDI GARSREDVEQ HGIEVGNMIT PYSEFETLAN SKYLTAKAFD
     NRYGCAVAVE VLKNLKDENL GINLYAGATV QEEVGLRGAK VAAQTIKPDL AIAVDVCVPY
     DIPGMSGQTS ETALGNGPVV IMMDASSIAH QGLRQHIKEV AKKHYISVQW DTTPGGGTDA
     GSIHVANEGI PTITIGVALR YMHSNVSVLH TDDYENSVRL ITEIVRSLND ETYQQIVW
//
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