ID A0A1N6T2G3_9GAMM Unreviewed; 362 AA.
AC A0A1N6T2G3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=DegS peptidase. Serine peptidase. MEROPS family S01B {ECO:0000313|EMBL:SIQ47542.1};
GN ORFNames=SAMN05880558_103372 {ECO:0000313|EMBL:SIQ47542.1};
OS Aeromonas sp. RU39B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1907416 {ECO:0000313|EMBL:SIQ47542.1, ECO:0000313|Proteomes:UP000186911};
RN [1] {ECO:0000313|EMBL:SIQ47542.1, ECO:0000313|Proteomes:UP000186911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU39B {ECO:0000313|EMBL:SIQ47542.1,
RC ECO:0000313|Proteomes:UP000186911};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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; FTMJ01000003; SIQ47542.1; -; Genomic_DNA.
DR RefSeq; WP_076575008.1; NZ_FTMJ01000003.1.
DR AlphaFoldDB; A0A1N6T2G3; -.
DR STRING; 1907416.SAMN05880558_103372; -.
DR InParanoid; A0A1N6T2G3; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000186911; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011783; Pept_S1C_DegS.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02038; protease_degS; 1.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
FT DOMAIN 253..344
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 98
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
FT ACT_SITE 207
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611783-1"
SQ SEQUENCE 362 AA; 38635 MW; C4D6DB96D3332E07 CRC64;
MKISPFLSYL GKAIGFGLTL ALFLLLLFPS LRGGAPLTNT SGRDLSFAYA ANRAGPAVVN
IYTRSFSRSD NNQTELRPQG LGSGVIMSER GHILTNYHVI AEADQIIVAL QDGRIFTAEL
VGTDKLTDLA VLSIEADALP VIPQNTDNQP EVGDVVLAIG NPYNVGQTIT QGIISATGRI
GLSSMGPESN GRQDLLQTDA AINAGNSGGA LVNTRGDLVG INTAAYHIDG NQESYGISFA
IPYKLAKRIM DELIRNGRVI RGYLGISSIE INPLVARMMK LGDLQGLVVE SLDPSGPASK
AGMQRGDVLL KINGAAIKSI RSAMDQIVET RPGSKLTFTL VRDGKTIDLP VTIEEDMRYP
QR
//