ID Q022I7_SOLUE Unreviewed; 428 AA.
AC Q022I7;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Fervidolysin. Serine peptidase. MEROPS family S08A {ECO:0000313|EMBL:ABJ84113.1};
DE Flags: Precursor;
GN OrderedLocusNames=Acid_3135 {ECO:0000313|EMBL:ABJ84113.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84113.1};
RN [1] {ECO:0000313|EMBL:ABJ84113.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84113.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP000473; ABJ84113.1; -; Genomic_DNA.
DR AlphaFoldDB; Q022I7; -.
DR STRING; 234267.Acid_3135; -.
DR KEGG; sus:Acid_3135; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_640761_0_0_0; -.
DR InParanoid; Q022I7; -.
DR OrthoDB; 184152at2; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..428
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004162886"
FT DOMAIN 142..386
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 368
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 428 AA; 44620 MW; 93F74ED2203EC6BA CRC64;
MKRRVLLLVL LCALAVPAEA AIRLIVRVQG GAPVLQAACL LLGCDVQYPL GDDEGQLVLV
TVPLNLTANL LLNVPGVLRV EVDTVGQTSG ATQSGAPAAL YDATPVSYFG TTVREGYVKQ
PAAQIIGLAA TQNRFGVRGA GIVAVIDTGV DSSHPALAGS LVPGYDFTRN RAGADEKGDV
GQSTTAVIDQ STTAVVDQST TAVIDQYSAA ALNQPQYQAF GHGTMVSGVV HLVAPGAMIM
PLKAFHADGT GYASDVIRAV YFAVHHRARI LNMSFSFQSS PMELQLALTY AKLNGVISVA
AAGNEGRETM VYPAGYSGTV MGVASTSNSD TLSTFSNYGQ RLVWVGAPGE GIVTLYPYGT
YAATWGTSFS APFAAGAAAL LLDVQAMCGE PQAADSLSHA RYINPDLGYG RLDLYQAVQA
WRRAAGLQ
//
