ID   A0A1H7S543_9BURK        Unreviewed;       530 AA.
AC   A0A1H7S543;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Kumamolisin. Serine peptidase. MEROPS family S53 {ECO:0000313|EMBL:SEL66637.1};
GN   ORFNames=SAMN05192542_11143 {ECO:0000313|EMBL:SEL66637.1};
OS   Paraburkholderia caballeronis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=416943 {ECO:0000313|EMBL:SEL66637.1, ECO:0000313|Proteomes:UP000199120};
RN   [1] {ECO:0000313|Proteomes:UP000199120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26416 {ECO:0000313|Proteomes:UP000199120};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FOAJ01000011; SEL66637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7S543; -.
DR   STRING; 416943.SAMN05445871_3521; -.
DR   OrthoDB; 9002785at2; -.
DR   Proteomes; UP000199120; 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; 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.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
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:UP000199120};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   DOMAIN          183..530
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        255
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        259
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        457
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         494
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         495
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         508
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         510
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   530 AA;  53893 MW;  CBDF952DCCC49BF3 CRC64;
     MTRHPVTGSN HPAPAGAQCI GACDPAERFD VVLILRRQAG DAFRDLVDRL AAGDRSAQPV
     SRDEYERRFG ASADDVARVA QFAQAHGLSV AHADPAARRV VLSGTVQQYN AAFGIDLQRF
     EHQVGQIKYR FRQPSGPVHL PDDVHDVVTA VLGLDDRAKA RPHFRIGSTI RPPIRPARAV
     SGAFTPLQLA QLYDFPAGDG GGACIALIEL GGGYREADLS AYFGALGVGA PKVEAVSVDQ
     AANAPTGDPN GPDGEVTLDV EIAGALAPAA LIAVYFAPNS EAGFVDAVSA ALHDRGRKPS
     VVSISWGAPE SAWSQQTIAA LNDALQTAVA LGVTVCVASG DSGSTDGVGD GAEHVDFPAS
     SPYALGCGGT RLSAGNGQIV RETVWGGGAP EGGATGGGVS ATFALPAWQK GLGIVRGNNG
     SGALVRRGVP DVAANADPAT GYLVHVGGED TVVGGTSAVA PLWAALIARI NATRGKPAGF
     VNALLYRQPS AFNDITSGNN GDFSAAPGWD ACTGLGTPVG SKVAAVLGAA
//