ID B8D248_HALOH Unreviewed; 653 AA.
AC B8D248;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ACL69275.1};
GN OrderedLocusNames=Hore_05170 {ECO:0000313|EMBL:ACL69275.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL69275.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL69275.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL69275.1; -; Genomic_DNA.
DR RefSeq; WP_012635463.1; NC_011899.1.
DR AlphaFoldDB; B8D248; -.
DR STRING; 373903.Hore_05170; -.
DR KEGG; hor:Hore_05170; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_419652_0_0_9; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000000719; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
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; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
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:UP000000719};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 264..531
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 289..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 485
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 653 AA; 71147 MW; 3FAAA10CD3E1A150 CRC64;
MDSKKYKVLL TAFIVIGILL FLPACSPEPD TGYKYYDIYG WVTEYNSGDP IKDAFVYIAG
QTAYTDETGY YHISNIPEGV HTWRVSADGY QGYSETIEVS SDLKVSIKLF PIGDGNVSGK
VTVNNNTGYQ RVDVSTASTS NNGSAVIFNK SSDGIQYKEN EILVKYKNEV STLSTNSLEN
NNGVQIMGTR ELPDGKVKHY RIPEDKTVSE MVDYYNNLPE VEWAQPNYIY HISAIPDDEY
YIYEQRGHII TNLEAAWDVE KGDNSVTVAV VDSGIIPDHP DLAGNLVPGH DFVDDDNDPT
DKTPESNSGS HGTHVAGIIG AVTNNGTGVA GVNWDVNILP VRVMGTDGSG FTDVIADGIR
YAVNNNVDII NLSLGVDPSR LENGSDPYMD DAINYAVNNG VIVIAAAGNG GSDSIGDSYV
DYPANMDSTI AVGAVDFNKD IASFSNYGQN LDLVAPGVGI YSTWGYYDGY NYETISDYYN
MSGTSMATPY VSGIAALLLA NGVPSYEVRN RLTSTAVDLG GTGWDQYYGY GLVDAYGALL
GKKLSKPYVM AAEFDETTNT VYPRSEIVQV NDDGTYSLQN VTPGEWYIIA YRDVDDNGYI
DAGDYYGETS NTYSINTDTS LKDINVNMYY VTGYNTSTSL KINGIAEIEE VNN
//
