ID Q81DP0_BACCR Unreviewed; 397 AA.
AC Q81DP0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=Thermitase {ECO:0000313|EMBL:AAP09280.1};
DE EC=3.4.21.66 {ECO:0000313|EMBL:AAP09280.1};
GN OrderedLocusNames=BC_2316 {ECO:0000313|EMBL:AAP09280.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP09280.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP09280.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP09280.1; -; Genomic_DNA.
DR RefSeq; NP_832079.1; NC_004722.1.
DR RefSeq; WP_000790938.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81DP0; -.
DR KEGG; bce:BC2316; -.
DR PATRIC; fig|226900.8.peg.2343; -.
DR HOGENOM; CLU_011263_15_6_9; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034084; Thermitase-like_dom.
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; 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:UP000001417};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 139..366
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 397 AA; 42306 MW; C9E71CFBF848BC81 CRC64;
MKNKIIVFLS VLSFIIGGFF FNTNTSSAET SSTDYVPNQL IVKFKQNASL SNVQSFHKSV
GANVLSKDDK LGFEVVQFSK GTVKEKIKSY KNNPDVEYAE PNYYVHAFWT PNDPYFNNQY
GLQKIQAPQA WDSQRSDPGV KVAIIDTGVQ GSHPDLASKV IYGHDYVDND NTSDDGNGHG
THCAGITGAL TNNSVGIAGV APQTSIYAVR VLDNQGSGTL DAVAQGIREA ADSGAKVISL
SLGAPNGGTA LQQAVQYAWN KGSVIVAAAG NAGNTKANYP AYYSEVIAVG STDQSDRKSS
FSTYGSWVDV AAPGSNIYST YKGSTYQSLS GTSMATPHVA GVAALLANQG YSNTQIRQII
ESTSDKISGT GTYWKNGRVN AYKAVQYAKQ LQENKAS
//
