ID A0A254Q0T7_9BURK Unreviewed; 477 AA.
AC A0A254Q0T7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:OWS72413.1};
GN ORFNames=CBI30_01180 {ECO:0000313|EMBL:OWS72413.1};
OS Polynucleobacter aenigmaticus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1743164 {ECO:0000313|EMBL:OWS72413.1, ECO:0000313|Proteomes:UP000198104};
RN [1] {ECO:0000313|EMBL:OWS72413.1, ECO:0000313|Proteomes:UP000198104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-K35W1 {ECO:0000313|EMBL:OWS72413.1,
RC ECO:0000313|Proteomes:UP000198104};
RA Hahn M.W.;
RT "Polynucleobacter sp. MWH-K35W1 isolated from the permanently anoxic
RT monimolimnion of a meromictic lake.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWS72413.1}.
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DR EMBL; NGUO01000002; OWS72413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254Q0T7; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000198104; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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; 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; PF13180; PDZ_2; 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};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..477
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013191299"
FT DOMAIN 87..159
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 423..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 51990 MW; 460DD49C0C48C093 CRC64;
MRVFFKNFAL VSVGLIAGVA ATIQLSATAQ QGATLPLDEL RTLSNVFAQI KREYVEPIED
KQLLTDAVKG MVSSLDPHST YLDKKDFSEM QEQTSGKFAG LGIEITSEDG VVKVLNPIED
SPAARAGLQA GDLITRLDDK PVRGMSLDKA VRTMRGTPGT KITLTVFRKS EERSFPVTIT
RAEIKVQSVK AKILDNNIAW VRVTSFQERT VPDLAKKLAE LANQDPKMKG IILDLRNNGG
GLLQGAVGVA AAFLPADAVI VSTKGQTPDA KQVFNATPAM YRLSEPGDPL ASVPAIYKKL
PMVVLVNAYS ASASEIVAGA LQDYKRATII GKTTFGKGSV QTVRPLSNDS ALKITTAYYY
TPTGKSIQAY GIKPDIAVDQ NKDGDPDDVL ITREIDSEKH LRNKQSSEEK LIADREKRRL
EELQRIEEKN AKKTPEEKEK DKTKKPVELG GADDFMLTQA VAFINGEPVK RSASKLE
//
