ID A4JM62_BURVG Unreviewed; 579 AA.
AC A4JM62;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Sedolisin, Serine peptidase, MEROPS family S53 {ECO:0000313|EMBL:ABO57365.1};
DE EC=3.4.21.101 {ECO:0000313|EMBL:ABO57365.1};
GN OrderedLocusNames=Bcep1808_4399 {ECO:0000313|EMBL:ABO57365.1};
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO57365.1, ECO:0000313|Proteomes:UP000002287};
RN [1] {ECO:0000313|Proteomes:UP000002287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) 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};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000615; ABO57365.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JM62; -.
DR MEROPS; S53.001; -.
DR KEGG; bvi:Bcep1808_4399; -.
DR eggNOG; COG4934; Bacteria.
DR HOGENOM; CLU_012501_0_0_4; -.
DR Proteomes; UP000002287; Chromosome 2.
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; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032,
KW ECO:0000313|EMBL:ABO57365.1};
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:UP000002287};
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_5002671039"
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; 60511 MW; 586771C3B0270D8C CRC64;
MKRNARFALS LPSPRRLACA WPLVFAAGAA HASTDWVDTH TKAFLTGPQL MARSTAPSLE
LAAGETADIV VSLKLRNAAQ LKQLARDVNR PGNAHYGQYL THEQFLADYA PTEAQVKSVV
DYLRKSGFVN IEVAPNRLLV SAHGTAGTVK TAFNTSLVHF QYAGRAGFAN ASTAQVPRAL
GDVVGSVLGL QNVARARPML RIGNVAKPQA LAAGTATGHY PKEFPGLYNA TGVPTAAGVT
VGIVTIGGVS QTLQDLKQFT SSNGYGTVAT QAVKTNGTGT SGSYSDDQDG QGEWDLDSQS
IVGSAGGQVG KLVFYMADLN AAGNTGLTQA FNRVVSDNTA KVINVSLGWC ETDANADGTL
DAEEQIFTTA AAQGQTFSVS SGDEGVYECN NRGYPDGSNY TVSWPAASPH VLAIGGTTLY
TTSAGAFSNE TVWNEGLDGN GKLWATGGGV STILPAPAWQ SGSNRRLPDV SFDAAQSTGA
YIYNYGQLQQ IGGTSLAAPI FTGFWARLLA ANGTGLGFPA ARFYARIPSN PSLVRYDVVS
GNNGYQGYGY TAGTGWDYPT GFGSLNVTNL NKLIQSGGF
//
