ID A0A1U9K9U4_9BACL Unreviewed; 430 AA.
AC A0A1U9K9U4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=B0W44_14540 {ECO:0000313|EMBL:AQS56786.1};
OS Novibacillus thermophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Novibacillus.
OX NCBI_TaxID=1471761 {ECO:0000313|EMBL:AQS56786.1, ECO:0000313|Proteomes:UP000188603};
RN [1] {ECO:0000313|EMBL:AQS56786.1, ECO:0000313|Proteomes:UP000188603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-1 {ECO:0000313|EMBL:AQS56786.1,
RC ECO:0000313|Proteomes:UP000188603};
RX PubMed=25951858; DOI=10.1099/ijs.0.000306;
RA Yang G., Chen J., Zhou S.;
RT "Novibacillus thermophilus gen. nov., sp. nov., a Gram-staining-negative
RT and moderately thermophilic member of the family Thermoactinomycetaceae.";
RL Int. J. Syst. Evol. Microbiol. 65:2591-2597(2015).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP019699; AQS56786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9K9U4; -.
DR SMR; A0A1U9K9U4; -.
DR STRING; 1471761.B0W44_14540; -.
DR KEGG; ntr:B0W44_14540; -.
DR Proteomes; UP000188603; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07487; Peptidases_S8_1; 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; 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; 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; 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:UP000188603};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 124..399
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 296..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 168
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 363
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 430 AA; 46524 MW; C4023A871C6A33B6 CRC64;
MNPLFKGWEQ KAVQVLDRTL ADTLPGVKSE STLPVIIEMT PNAKEEERQE IKQLCQQRKR
DEIVNELKYI PMVTATICQD TLREAAHHPG VKRIFYDQQV RAYLDVAVPT VAADEAHARW
GLTGKGITVA VLDTGIEAHD DLTKPENRLA GFNDLVGNET ESYDDNGHGT HVAGIIAGNG
YRSDGKYVGS APEANLVGVK VLDNRGSGQV STIMRGIDWC IQEKEQYNIR VINLSLGGPA
TEPYTDDPLS RMVEQAWHNG IVVCAAAGNE GPEPGTIGTP GFHPSIVTVG ATYDQNTETT
EDDKESEFSS RGPTVDHLNK PDVLAPGEKI VSLLAENSPL NRRIERGDLS SPLDGYVELS
GTSMATPLCA GVAALLIQHN ESLSPNDVKS ILVSSSTHLK GSQPGYVNVV SALKLAEVYL
EYGSHDVYSS
//
