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Database: UniProt
Entry: A0A1N7SS77_9BURK
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ID   A0A1N7SS77_9BURK        Unreviewed;       579 AA.
AC   A0A1N7SS77;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pseudomonalisin {ECO:0000313|EMBL:SIT49786.1};
DE            EC=3.4.21.100 {ECO:0000313|EMBL:SIT49786.1};
GN   Name=pcp {ECO:0000313|EMBL:SIT49786.1};
GN   ORFNames=BN2475_1790002 {ECO:0000313|EMBL:SIT49786.1};
OS   Paraburkholderia ribeironis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1247936 {ECO:0000313|EMBL:SIT49786.1, ECO:0000313|Proteomes:UP000187012};
RN   [1] {ECO:0000313|EMBL:SIT49786.1, ECO:0000313|Proteomes:UP000187012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM7296 {ECO:0000313|EMBL:SIT49786.1,
RC   ECO:0000313|Proteomes:UP000187012};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
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DR   EMBL; CYGX02000179; SIT49786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7SS77; -.
DR   STRING; 1247936.BN2475_1790002; -.
DR   OrthoDB; 5481934at2; -.
DR   Proteomes; UP000187012; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU01032};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032,
KW   ECO:0000313|EMBL:SIT49786.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187012};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..579
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013292336"
FT   DOMAIN          218..577
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        293
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        297
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        495
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         537
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         538
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         555
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         557
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   579 AA;  61153 MW;  E89579A06E9DA6DC CRC64;
     MKRNYRLALP LPSPRRLACA VPLVFSAAAA HATTDWVDTH TNAFLTGPQL MARNAAPSLE
     LADGEITDIV VSLNLRNAAQ LEQLGHDVNQ PGNAHYRQYL TPEQFLVSYA PTEAQVKSVV
     DYLRKSGFVN VEVAPNRLLV SARGTAGTVK TAFNTSLVHY QDASRSGFMN ASKAQVPRAL
     GDAVGSVLGL QNIARAQPML RIGNVEKPQA LAAGTATGHY PKEFPGLYNA TGVPTAAGVT
     VGIITMGGVS QTLKDLEQFT SSNGYGTVTT QTEKTNGTGT TGSYSDNPFL QSEWDLDSQS
     IVGSAGGQVG KLIFYMADQN AAGDTGLTQA FNRAVWDNTA KVINVSLGWC ETDADKDGTI
     DAQEQIFTTA AAQGQTFSVS SGDEGAYECN NRGFPDGTNY TVSWPAASPH VLAIGGTTLY
     TTSTGAFSNE TVWNEGLDPT GKLWATGGGV STILPAPVWQ SGSNRRLPDV SFDAALSTGA
     YIYNYGQLQQ VGGTSLAAPI FTGFWARLLA ANGTSLGFPA GDLYRAIPSN PSLVRYDVVS
     GNNGYQGLGY KAGTGWDYPT GFGSLSITNL NELIRSGRF
//
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