ID A0A166T6B5_9RHOB Unreviewed; 446 AA.
AC A0A166T6B5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:KZY02790.1};
GN ORFNames=A3721_19235 {ECO:0000313|EMBL:KZY02790.1};
OS Sulfitobacter sp. HI0023.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZY02790.1, ECO:0000313|Proteomes:UP000077323};
RN [1] {ECO:0000313|EMBL:KZY02790.1, ECO:0000313|Proteomes:UP000077323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0023 {ECO:0000313|EMBL:KZY02790.1,
RC ECO:0000313|Proteomes:UP000077323};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) 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:KZY02790.1}.
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DR EMBL; LWEQ01000171; KZY02790.1; -; Genomic_DNA.
DR RefSeq; WP_067926625.1; NZ_LWEQ01000171.1.
DR AlphaFoldDB; A0A166T6B5; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000077323; 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 Reference proteome {ECO:0000313|Proteomes:UP000077323};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 88..156
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 392..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 47744 MW; 4DEE2EAEA3BAA45B CRC64;
MKKFVMAALG GTLAGVIATT QIAGPLLAQE SVKINNVYEQ LDLFGDIFER IRAQYVEEVD
PADLIEAAIN GMLTSLDPHS SYLSPRDALK MREQTRGEFG GLGIEVTQED GFVKVVSPID
GTPAAEAGIE AGDFITHVDG ESLLGLLLDD AVEMMRGPVG SEIVITVVRE GEQEPFDVTI
VRDTIQLTAV RARTEGKSAV LRVTTFNEQT FPKLKEGLEE QIEAADGIEN LNGIVLDLRN
NPGGLLSQAI AVSDAFLEEG EIVSTRGRDP ADGDRVNATP GDLAEGKPIV VLINGGSASA
SEIVAGALQD HRRAIVVGTK SFGKGSVQTV MPLRSDGAMR LTTARYYTPS GRSIQALGVS
PDIVVAQPPV VPGNEEEEDE SLARPLRSEA DLRGSLNNDS LSDDQIKQIE EDREKAEQAA
QLREEDYQLA YAIDILKGLS ALGPRD
//
