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
//