ID G2SWI2_ROSHA Unreviewed; 595 AA.
AC G2SWI2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Peptidase S8/S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:AEN96266.1};
GN OrderedLocusNames=RHOM_05735 {ECO:0000313|EMBL:AEN96266.1};
OS Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN96266.1, ECO:0000313|Proteomes:UP000008178};
RN [1] {ECO:0000313|EMBL:AEN96266.1, ECO:0000313|Proteomes:UP000008178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183
RC {ECO:0000313|Proteomes:UP000008178};
RX PubMed=26543119; DOI=10.1128/genomeA.01286-15;
RA Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL Genome Announc. 3:E0128615-E0128615(2015).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003040; AEN96266.1; -; Genomic_DNA.
DR RefSeq; WP_014079311.1; NC_015977.1.
DR AlphaFoldDB; G2SWI2; -.
DR STRING; 585394.RHOM_05735; -.
DR GeneID; 77458777; -.
DR KEGG; rho:RHOM_05735; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_025670_0_0_9; -.
DR OrthoDB; 9762689at2; -.
DR BioCyc; RHOM585394:G1H02-1159-MONOMER; -.
DR Proteomes; UP000008178; Chromosome.
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; IPR022398; Peptidase_S8_His-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; 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:UP000008178};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 4..101
FT /note="Csp protease B prodomain"
FT /evidence="ECO:0000259|Pfam:PF18425"
FT DOMAIN 127..367
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 457..569
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 523
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 595 AA; 64647 MW; 12B7C56C59612DB3 CRC64;
MPNEKMENLL NLALAATQEE REKSLELDIG YDSAEQTWEV IVKFVGTTEE LEALLFKNFP
EEYPRIRLTN LQNEYAVLVL PEHLVEPVAA LDKIEYMEKP KLLFFAVDNG KRASCITQLQ
ERTGLSGAGV LVAVIDSGID YAHPDFRRAD GTTRIVSLWD QTIPASGGLS APAGYFLGTE
YDEARINEAL AQPTEQQRYA VCPSRDASGH GTHVAGIAAG NGRASEGRYR GVAYESDLLI
VKLGNQREGA FPRTTELMQA VDYCIRKAQE RQQPVAINLS FGNNYGSHTG TSLIETYLDD
LANYWKSSIV IGSGNEGAAA THTAGALGMG QAENVEFAVS AYESALNLQI WKSYADEMAV
LLIHPGGMQI GPIRQIQGSQ RFTLGQTQIL LYYGEPSPYS PYQEIYLDFL PVRDYVDSGI
WTVRLIPQRI VTGRYDMWFP AGGVLNEGTG FLLPREETTL TIPSTAAKVI TVGAYDARFG
QLAGFSGRGF TGNGQVKPDL AAPGVEITSC APGGGYTARS GTSMATPFVT GSAALLMEWG
IVRGNDVYLY GEKIKAYLIR GARPLGGGRA SGLLQEYPNP QVGWGTLCLS DSLPE
//
