ID Q5SLK7_THET8 Unreviewed; 689 AA.
AC Q5SLK7;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Serine protease, subtilase family {ECO:0000313|EMBL:BAD70109.1};
GN OrderedLocusNames=TTHA0286 {ECO:0000313|EMBL:BAD70109.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD70109.1, ECO:0000313|Proteomes:UP000000532};
RN [1] {ECO:0000313|EMBL:BAD70109.1, ECO:0000313|Proteomes:UP000000532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AP008226; BAD70109.1; -; Genomic_DNA.
DR RefSeq; WP_011227833.1; NC_006461.1.
DR RefSeq; YP_143552.1; NC_006461.1.
DR AlphaFoldDB; Q5SLK7; -.
DR EnsemblBacteria; BAD70109; BAD70109; BAD70109.
DR GeneID; 3168155; -.
DR KEGG; ttj:TTHA0286; -.
DR PATRIC; fig|300852.9.peg.286; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_380248_0_0_0; -.
DR PhylomeDB; Q5SLK7; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR017306; Peptidase_S8A_fervidolysi-like.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
DR PIRSF; PIRSF037882; Subtilisin_rel_fervidolysin; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000532};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..689
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004262905"
FT DOMAIN 164..421
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 591..665
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 376
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 689 AA; 73346 MW; 38C7DE487F22F672 CRC64;
MKKPLILSAL ALAALLSACS QAPRPTNASP TPGLVTTSEG VRHYQGQVVV GYEDESGLQE
AIRKLGAKEI ARIPELKAAL LEVPGDAVKA SRTLKGLPGL RYAEPHLAQV TPPKDDPVEL
PRGRESGLIP LGNPSDQILD ELPQYALDPR HLAAKAAWDR GFEGEGVVVA IIDDPADVTH
PDLAPNWAGK AYDPVTDTTY TSASGWLNFI QGLNAPADLY HGTYVASTVS APRDGQGIAG
LAPKTKFLPV AIFQPDYVGD FYVARGIVWA VNNGAQVLNN SWGGLGYGQL VKEAFDYALA
NGVVVVASAG NSYKDEVRTP AGYPGIIASA AADGNRNKTD FSTYGRHISS AAPGLDVLLA
NPTWLGGGYG LISGTSFSGP YTAAAAALVK AACPGATPYQ VRRALETTTW EKTFTREKGW
GHLHAGQLAE LLSQGCAALP AKGAVVRVKV EYFNERGTFP GLLADVILRG KGLKPGDPTD
PTPVYWARTD QNGEAWFYEI APGEYDIYVA GADLALTGGP PEERGTFVGT LVATPGSSAF
SPDSKLVRLN ASEVNLNPTD PYEPNDTLSQ AKPIAYGQTT QLAYIFGQPQ DYDYFQFTGS
AGDTIKARVY ARSSIGGTLD SYLYLLDENG QVLAENDDII FGQITDSEII FTLPQDGTYY
LVVTSYTIAN GGSDDSPFNK YRLELQKTN
//
