ID C5BRN2_TERTT Unreviewed; 465 AA.
AC C5BRN2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN OrderedLocusNames=TERTU_1184 {ECO:0000313|EMBL:ACR13448.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR13448.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR13448.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
CC -!- FUNCTION: Might be efficient in the degradation of transiently
CC denatured and unfolded proteins which accumulate in the periplasm
CC following stress conditions. {ECO:0000256|ARBA:ARBA00002610}.
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DR EMBL; CP001614; ACR13448.1; -; Genomic_DNA.
DR RefSeq; WP_015819562.1; NC_012997.1.
DR AlphaFoldDB; C5BRN2; -.
DR STRING; 377629.TERTU_1184; -.
DR KEGG; ttu:TERTU_1184; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_6; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000009080; 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; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 2.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ACR13448.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..465
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002948873"
FT DOMAIN 247..344
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 465 AA; 50090 MW; E4F466A04847C50E CRC64;
MRAASFFRFV CVLTVALAID VNAASYNLPD FRPLIEKTSP AVVKINTTTK ARQSEIELPP
GHQIPDIFRH LLEPRDLPRR EMHSMGSGFF ISADGYLLTN NHVVEDADQI VVRLVDRREY
KAIVIGRDPR SDLALLKVDE DKLPYLELAA KDDIQIGEWV VAIGSPFGLD FSASAGIVSA
IGRSIPTERN ENYVPFIQTD VAINPGNSGG PLFNLDGKVV GVNSQIYTRS GGSIGLSFAI
PSSVALNVVS QLKEKGRVDR GWLGVVIQEV DKDLADSFGL KKPAGALVAQ LEPTGPAAMS
GLLVGDIILR FDDQEILSSG DLPHAVGATP PDTEVPVLVM RKGKRKTLDV KVGRLSGHES
DAPAQVLADG NVVTDRLGLV VEPVDATVEE KWHLVGGVLV TQVDPQGAAA DAGISPGDVI
AQLGFEQIAT VDDYTRVMKA LPADDLVPIR FFRDGSPTFR TIRIE
//
