ID A0A0B6X065_9BACT Unreviewed; 564 AA.
AC A0A0B6X065;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=C-terminal processing peptidase {ECO:0000313|EMBL:CDM66918.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:CDM66918.1};
GN ORFNames=PYK22_02959 {ECO:0000313|EMBL:CDM66918.1};
OS Pyrinomonas methylaliphatogenes.
OC Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC Pyrinomonadaceae; Pyrinomonas.
OX NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM66918.1, ECO:0000313|Proteomes:UP000031518};
RN [1] {ECO:0000313|EMBL:CDM66918.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM66918.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Stott M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDM66918.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM66918.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA Stott M.B.;
RT "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT K22T.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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; CBXV010000008; CDM66918.1; -; Genomic_DNA.
DR RefSeq; WP_060635730.1; NZ_CBXV010000008.1.
DR AlphaFoldDB; A0A0B6X065; -.
DR STRING; 454194.PYK22_02959; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000031518; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:CDM66918.1};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000031518};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 88..159
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 375..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 62468 MW; 7681246DBA5FC58D CRC64;
MSKSFGIVAV FIIVASTLIG GALGKRLLPL RAGDRSTDAI QRIEEDYREA LNIISANYAG
EIDYERLNQT SIQGMLLTLD PHSNFFTRAE FQRLREDQES RFYGIGISIL RHRDGVYVQS
VVEGTPAARA GLRYGDRILE VDGQDARDWS TEQASRKIRG ERGEPVTLKI ERAGEQAPLY
LTIVRDAVPL PSIRLAFMIR PGIGYIGLTG GFTHTSADEL RRAIADLKRQ GMRQLILDLR
NNPGGLLEQA IGVAGQFLDY GQVIVSVRGR EYPEPKVYRN YERDPEQMPL VVLINRGSAS
ASEIVAGAIQ DHGRGLIVGE TSFGKGLVQR VFQLPFGTGL TLTTAKYYTP YGRLIQRQYT
SGSFYDYYTR RGANEMNSGP QTSRPGSPTI AAPEATPRPS PTGPAIRTAG GRLFYGGGGI
TPDIEVKPIE IDTPLRGRIF EAAFYFTRQL VAGQIQGLES YRIEKVQFNH VPRPTDYPVT
EKVLEAFREF LQRSPEFGVK PAQVDADLEF VKLRLRDEII TAAYGSEAGT RVLLESDPQL
LRAIEALPEA KRLAEAVRRG ESIG
//
