ID A0A0J1GEQ4_9FIRM Unreviewed; 766 AA.
AC A0A0J1GEQ4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=RHS_0097 {ECO:0000313|EMBL:KLU74002.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU74002.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU74002.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU74002.1};
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:KLU74002.1}.
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DR EMBL; JNGB01000001; KLU74002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1GEQ4; -.
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; cd07477; Peptidases_S8_Subtilisin_subset; 1.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
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; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..766
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038878957"
FT DOMAIN 226..453
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 123..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 267
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 418
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 766 AA; 84732 MW; 9F9F4FE7A9E5EFE3 CRC64;
MKRKMKISGK KVVSSCLVFA MMCQLVGSNN MMIANAENET DAETKTYIVM ADSSKEFNDV
TNRAAFSISE EDPELADNNI AVMELSPEEA EEMQQNDGLI VEEDIIISAN SLEEEIITEG
TEAETFFTES EEESQTTTAE TEVTEETEIT EKSSVSTETI ENTDNLTLEE TEEPETEDSE
KAKRMEYKLK LREARNNARD TEVEADWNLQ AINADEVNIN ARSIDKVKVA LLDSGVDYND
GIDLSDSINF VDEEDYVVPM YQDLTGHGTG IASIICANGE GGIKGVNPNV DLYSVKVLDG
ENKAPLSRII KGIYWCIDND VNIINMSFGT STYSNAMKKA VEDAYDAGIL MVGASGNNAD
KVEYPAAFKE VMAVASTNAE AEISSFSNTG KELDIAAPGE KIQTASFFGG SVVTHGTSIA
VPHVVGVASL LWEKDLSKTH EFIRQLIDTT SKNISNTDQC GLIDANYAMS MYEVFVQNFD
ESNIVREEMI PENPENPDIF SEVNEDETYV EGRWAGEGHK DLVDTGISNA GWDLSVQAVS
IIKEGVVYPD QKEVSNIYGY GAYPEYHGGV KWEKVKDKEI VPINFLSCYE LLTKIALKGG
DTSKFTNYKI VKGMDKRVFD KIKSKITITK FGDQPWSKIL AKYGNTKTNR KYFLWGAAIH
LVSDSFAHRI WYKDNGKVGK YIDHPDADKP SICKNRFKVA GDAVSSSVAS LVIDVEGDFP
DVGYAISDKF NNTFVRQDLY KCWIDVGGND RGIDNATIQK IKNASK
//
