ID A6LNY1_THEM4 Unreviewed; 452 AA.
AC A6LNY1;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:ABR31632.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:ABR31632.1};
GN OrderedLocusNames=Tmel_1797 {ECO:0000313|EMBL:ABR31632.1};
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Thermosipho.
OX NCBI_TaxID=391009 {ECO:0000313|EMBL:ABR31632.1, ECO:0000313|Proteomes:UP000001110};
RN [1] {ECO:0000313|EMBL:ABR31632.1, ECO:0000313|Proteomes:UP000001110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429
RC {ECO:0000313|Proteomes:UP000001110};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR31632.1, ECO:0000313|Proteomes:UP000001110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429
RC {ECO:0000313|Proteomes:UP000001110};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP000716; ABR31632.1; -; Genomic_DNA.
DR RefSeq; WP_012057990.1; NC_009616.1.
DR AlphaFoldDB; A6LNY1; -.
DR STRING; 391009.Tmel_1797; -.
DR KEGG; tme:Tmel_1797; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_0; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000001110; Chromosome.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
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; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Oxidoreductase {ECO:0000313|EMBL:ABR31632.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABR31632.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 248..339
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 452 AA; 49646 MW; 16F872F4F3467CE7 CRC64;
MTKRLGILIL TVLAIFSFGY VNPNYESPIT KVVDEAAPAV VKIEATVYST SYIDPFIEEF
FKRWFGDIPK QYQQKGTSLG SGFIFEKEGY ILTNFHVVDG AENIKVSLLD GKEFSAEFIG
GDKELDIAIL KIDPKNQELP VLEFGDSDKL KIGEWAIAIG NPLGFQHTVT VGVISATGRK
IPKPDNDGYY TNLIQTDAAI NPGNSGGPLL NIHGQVIGIN TAIIAPSEAM NIGFAIPINT
AKRFIDSIIK TGKAEKAYLG VYMQTVTKEL AKALGLKTDK GVFISQVIKD SPAEKAGLKD
GDVIIEVEGL SVTSASELKS IIHNYTPGSK IKIIVNRKGK IIKFEVTLGK SKETEKVTSA
KEFMGLTVKD ITNADREEYQ IPEEISGVVV KNSKISYISE GYVIFRIAIN GQKYEIRNIN
DWNKVISKIN KGNYVALFYY YKGATGVFSF GY
//