ID G8N4J8_GEOTH Unreviewed; 453 AA.
AC G8N4J8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Protease {ECO:0000313|EMBL:AEV19062.1};
GN ORFNames=GTCCBUS3UF5_17500 {ECO:0000313|EMBL:AEV19062.1};
OS Geobacillus thermoleovorans CCB_US3_UF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV19062.1, ECO:0000313|Proteomes:UP000005636};
RN [1] {ECO:0000313|EMBL:AEV19062.1, ECO:0000313|Proteomes:UP000005636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV19062.1,
RC ECO:0000313|Proteomes:UP000005636};
RA Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT CCB_US3_UF5.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; CP003125; AEV19062.1; -; Genomic_DNA.
DR RefSeq; WP_011231013.1; NC_016593.1.
DR AlphaFoldDB; G8N4J8; -.
DR SMR; G8N4J8; -.
DR KEGG; gte:GTCCBUS3UF5_17500; -.
DR PATRIC; fig|1111068.3.peg.1696; -.
DR HOGENOM; CLU_011263_15_6_9; -.
DR Proteomes; UP000005636; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034084; Thermitase-like_dom.
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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..453
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038389629"
FT DOMAIN 197..440
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 392
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 453 AA; 49888 MW; 9CD9DE39A40533D9 CRC64;
MKRRYRIWAA ASAVVALLVA AAVLGRPAPE ENAPAPPRLK PFDAEVAPTH PTVVALDSLS
AGEQLKQQLN KHPRIREILH NRRGDRSHYF ANEIVVRFRA LPSESRLQQM EAAIAGQFIK
QVDHVFVFRS REQTYEEMRR YFRSLPTVDY CEPHYIYMQN EWNKPAPVPN DSFYARYQWN
LPAIHTEDGW TLSRGKRNVP VAIIDSGVDL THPDLTRRLL PGYNVLADDR SPNDENGHGT
HVAGIIASQP NNGEGVAGMT WFNPIMAVKA LNADGYGTSI DVAKGIRWAV DHGAKVINLS
LGNYQPSSVL EEAIRYADAH DVVLVAASGN DSTSQASFPA AYPEVISVGA VNPDLSYALY
SNYGDYVDVV APGTNIASTF AGHRYAALSG TSMAAPHVTA LAALIRSVNP RLSNDEVRDI
ILESADDLGE RGKDPYYGYG LINVYRALEL AKQ
//
