ID   Y1059_STAS1             Reviewed;         350 AA.
AC   Q49YD7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Uncharacterized peptidase SSP1059;
DE            EC=3.4.-.-;
GN   OrderedLocusNames=SSP1059;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; AP008934; BAE18204.1; -; Genomic_DNA.
DR   RefSeq; WP_011302902.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49YD7; -.
DR   SMR; Q49YD7; -.
DR   STRING; 342451.SSP1059; -.
DR   PRIDE; Q49YD7; -.
DR   EnsemblBacteria; BAE18204; BAE18204; SSP1059.
DR   KEGG; ssp:SSP1059; -.
DR   PATRIC; fig|342451.11.peg.1058; -.
DR   eggNOG; COG0006; Bacteria.
DR   HOGENOM; CLU_017266_4_2_9; -.
DR   OMA; IHEWPYL; -.
DR   OrthoDB; 415910at2; -.
DR   Proteomes; UP000006371; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..350
FT                   /note="Uncharacterized peptidase SSP1059"
FT                   /id="PRO_0000299431"
FT   BINDING         214
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         289
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         318
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         332
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         332
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   350 AA;  39215 MW;  71E5CD20ECDEB26C CRC64;
     MKLEQITEEL KSQQADAAWI TTPLNIFYFT GYLSDPHERL LALLIKSNGE QVLFCPQLEV
     EEVRASPFNG EVIGYLDTEN ALDKYDIKFN KLLVESAHLT LQRQRELIDA FGVQSFGDID
     QTIKTLRNIK SDSEIEKIKK ACELADKCIE IGVSFLKEGV TERQVVNHIE YEIKAYGVNE
     MSFDTMVLFG DHAASPHGTP GDRQLKKDEF VLFDLGVIYE NYCSDMTRTV KFGTPDAKAQ
     EIYDVVLKAE KEAIAAIKPG VTIKDVDDIA RNIITEAGYG EYFPHRLGHG LGLEEHEYQD
     VSSTNTNEFK AGMVITVEPG IYVPGVAGVR IEDDILVTEN GNESLTGYEK