ID A0A2A4W052_9PROT Unreviewed; 444 AA.
AC A0A2A4W052;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:PCI63673.1};
GN ORFNames=COB37_04400 {ECO:0000313|EMBL:PCI63673.1};
OS Kordiimonadales bacterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales.
OX NCBI_TaxID=2030814 {ECO:0000313|EMBL:PCI63673.1, ECO:0000313|Proteomes:UP000217879};
RN [1] {ECO:0000313|Proteomes:UP000217879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-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:PCI63673.1}.
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; NVTU01000010; PCI63673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4W052; -.
DR Proteomes; UP000217879; 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..444
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012065453"
FT DOMAIN 84..148
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 345..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 49031 MW; 3F04E2BFFA634A40 CRC64;
MRKLVTGALL ALMMTVPGHA QKQQSQDEFY EQLDLLMRVL ERVRSEYVDE VDDKKIVEAA
IQGVLRSLDP HSTYLNPEVY EQVRVQIQGE YGGLGIEVQA DKGVVKVVSP IDDTPADEAG
VLGGDYITHI DGEAILGQTL SEAIKKMRGP VDTPVVITIV REGEPEPFDI EIVRRKIMVR
AVRHRIEDET IGYVRVTTFN MQSGRLVEEA VNAIVDELGP DLDGLILDLR NNPGGLLNEA
IRISDVFLDR GEIVSTKGRR RQNNNRWHAT SGDLLNGIPM VVLTNAYSAS ASEIVAGALQ
DHRRAIILGD RTFGKGTVQS EIQLGRSGSQ AIRLTTARYF TPSGRSIQER GVEPDIELLQ
PRQKGQRGKP RREADISGHI TNDQQGLDRT GEKDGKATAK KISTTDPVTA NTVQEPVDVQ
LRYAIKLLKN MSNLPKPQLA EARS
//
