ID A6L8X8_PARD8 Unreviewed; 507 AA.
AC A6L8X8;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ABR42142.1};
GN OrderedLocusNames=BDI_0359 {ECO:0000313|EMBL:ABR42142.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR42142.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR42142.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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DR EMBL; CP000140; ABR42142.1; -; Genomic_DNA.
DR RefSeq; WP_005862015.1; NZ_LR215978.1.
DR AlphaFoldDB; A6L8X8; -.
DR STRING; 435591.BDI_0359; -.
DR PaxDb; 435591-BDI_0359; -.
DR KEGG; pdi:BDI_0359; -.
DR PATRIC; fig|435591.13.peg.354; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_10; -.
DR BioCyc; PDIS435591:G1G5A-370-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR025926; PDZ-like_dom.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF12812; PDZ_1; 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 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABR42142.1};
KW Protease {ECO:0000313|EMBL:ABR42142.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000566};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..507
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002696707"
FT DOMAIN 332..386
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 250
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 507 AA; 53791 MW; 26E2D24E1944A511 CRC64;
MKNIWKNVLG VALIAAISSG AAIGTSTYLM NKNQRPAELA SGVENTFKQP YRLTNYGTVA
AENIDFTTAA ESAIHGVVHI KATANAQASN GDGGQQYMDP FEYFFGFGGR GGFQRPQQQP
RVGAGSGVII STDGYIITNN HVIDGADELE VTLNDNRKFP AKIIGADPTT DIALIKIEAT
DLPTIPFGDS EKLKVGEWVL AVGNPFNLTS TVTAGIVSAK SRGNIGAGGK DRSKIESFIQ
TDAAVNPGNS GGALVNTKGE LVGINTAIYS ETGNFAGYSF AVPISIAGKV ANDLKQFGTV
QRAVLGVLIQ DPQYVPDAEK EKVKVFEGAY VGGFAERSSA KEAGIEKGDV IVAVNGVKIK
SSSALQEQIS KYRPGDKVEL TINRNGSTKK FTVELRNAQG STKVVKGGDS AEVMGAAFKA
LNDEQKRKLG VSYGIEVTGL TSGKLKDAGI KKGFIIMIVN NQKISAPEDL EKIVESILQG
RTEDQGLFIK GFYPNGRTKY YAIDLAE
//