ID A0A0J1FXW8_9FIRM Unreviewed; 579 AA.
AC A0A0J1FXW8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHS_5959 {ECO:0000313|EMBL:KLU68214.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU68214.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU68214.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU68214.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLU68214.1}.
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DR EMBL; JNGB01000212; KLU68214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1FXW8; -.
DR PATRIC; fig|1504536.3.peg.3122; -.
DR Proteomes; UP000036477; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07478; Peptidases_S8_CspA-like; 1.
DR Gene3D; 2.60.120.1290; -; 1.
DR Gene3D; 3.30.70.2980; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR041365; CspB_prodomain.
DR InterPro; IPR034045; Pep_S8_CspA-like.
DR InterPro; IPR017310; Pept_S8A_subtilisin_clostridia.
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; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF18425; CspB_prodomain; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PIRSF; PIRSF037894; Subtilisin_rel_CspABC; 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}; Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 5..92
FT /note="Csp protease B prodomain"
FT /evidence="ECO:0000259|Pfam:PF18425"
FT DOMAIN 119..306
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 447..568
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 513
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 579 AA; 63161 MW; B76E5C6D907D0C43 CRC64;
MATDQKIENL LNLALDATPE EREKSLTLDV GYDPVDQKWE IIVKYSGDIS RLESEDIQVV
ELINEYAIIT LPESKIAYLA AQPEVEFIEK PKRLFFSVNQ GRAASCMNVL QTPAFNLNGE
GIIVAVIDSG VDYTHPDFRN PNGSTRILNI WDQTLPGNPP KGYKIGTEFD QAQINAALNP
EAEGERSAQA VPSRDLSGHG TQVLGIAAGN GRASNGRYRG VAYASDIIVV KLGLARPNSF
PRTTELMQAL DYVIRKSIEY QKPVAINLSF GTVYGSHDGS GLLETYIDDI SNLWKSTISV
GTGNEGSTGG HTSGILKNNV PVEIQLGIVN NELSINLQIW KSYVDEFEIT IVHPSGQVVG
PLQEVLGPQR YIAGETELLV YYGEPSPYST SQEIYIDFIP RDTYIDSGIW RLIFTPKRIV
EGRYDVWLPA SAAVGIGTRF YQPTVETTLT IPSTARKVIA VGAYDSRLLT YAPFSGRGYN
RDSSQVKPDV SAPGVDITTA TPGGGYTTVS GTSFATPFVT GAAAMLMQWG IVMGNDPYLY
GEKVKAYLIR GARPLNVERV YPNPTLGYGT LCVKDSFPG
//
