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Database: UniProt
Entry: A0A127QT39_9BURK
LinkDB: A0A127QT39_9BURK
Original site: A0A127QT39_9BURK 
ID   A0A127QT39_9BURK        Unreviewed;       645 AA.
AC   A0A127QT39;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Pseudomonalisin {ECO:0000313|EMBL:AMP12772.1};
GN   Name=pcp {ECO:0000313|EMBL:AMP12772.1};
GN   ORFNames=CPter291_0486 {ECO:0000313|EMBL:AMP12772.1};
OS   Collimonas pratensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP12772.1, ECO:0000313|Proteomes:UP000074914};
RN   [1] {ECO:0000313|EMBL:AMP12772.1, ECO:0000313|Proteomes:UP000074914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter291 {ECO:0000313|EMBL:AMP12772.1,
RC   ECO:0000313|Proteomes:UP000074914};
RA   Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E., Cankar K.,
RA   Beekwilder J., van Veen A., de Boer W., van Veen J.A., Garbeva P.;
RT   "Exploring the genomic traits of fungus-feeding bacterial genus
RT   Collimonas.";
RL   Submitted (NOV-2015) 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; CP013236; AMP12772.1; -; Genomic_DNA.
DR   RefSeq; WP_062111740.1; NZ_CP013236.1.
DR   AlphaFoldDB; A0A127QT39; -.
DR   PATRIC; fig|279113.10.peg.484; -.
DR   Proteomes; UP000074914; Chromosome.
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; 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; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 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}; 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   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..47
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           48..645
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007278174"
FT   DOMAIN          253..640
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
FT   ACT_SITE        325
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        329
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   ACT_SITE        556
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         599
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         600
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         618
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT   BINDING         620
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ   SEQUENCE   645 AA;  66565 MW;  E38F096EA5837A03 CRC64;
     MKSETVTKTA VQTSARKSAA GFAIPRASAL SLALSLAFAS LSGVAHAAAD DSWVATKTKA
     FLPQVQAKQK SSAVDASVQT PAEAAVQMAQ GEPVHVTLSL NLRNEAKLDQ FLKDLHTPGS
     TAHRKYLTPA QFKAEYAPTE KDVATVVAHL RKAGFVNIKV APNRQLVSAS GTAATVQAGF
     HTALKRFQQD GRPVFANTDA AQVPAALGHI VGAVLGLQNV ELAHTNFVMQ APQQGRAAVL
     AKARTNATPV QTSHSPAEFP GIYNAGSTPT ASNTTVAVIS EGDLTQTISD LNTFTDSNNF
     ATINTNVVQT GADGSDYSDT SGMVEWNLDS QTIAGTTGGA VQQLIFYASP DMQFSSITAS
     YNQVVSDNLA KVINVSLGAC EAAANSDGTQ AADDNIFKQA VAQGQTFSVS TGDAGAYNCQ
     VSSISGAPGV PKNKSTYDVS EPASSPYVIA VGGTALYTNA GAYSSEIVWN EGLRAIGQYD
     AAGDVDNTKR IWATGGGYSK YEAAPSYQSG VTASGATTRG LPDIAFDAAS ASGANLVING
     STTNQNGNLY TVGGTSLAAP IFTGVWARLQ SANANGLGFP AASFYKYFPL AANASLLHDV
     TSGTNGYSSS YGFKAAKGWD AVTGFGSLNI GNLNAFVTNT ADFAR
//
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