ID G8N0U8_GEOTH Unreviewed; 406 AA.
AC G8N0U8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Serine protease Do {ECO:0000313|EMBL:AEV21184.1};
GN ORFNames=GTCCBUS3UF5_38860 {ECO:0000313|EMBL:AEV21184.1};
OS Geobacillus thermoleovorans CCB_US3_UF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV21184.1, ECO:0000313|Proteomes:UP000005636};
RN [1] {ECO:0000313|EMBL:AEV21184.1, ECO:0000313|Proteomes:UP000005636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV21184.1,
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP003125; AEV21184.1; -; Genomic_DNA.
DR RefSeq; WP_011232933.1; NC_016593.1.
DR AlphaFoldDB; G8N0U8; -.
DR MEROPS; S01.364; -.
DR KEGG; gte:GTCCBUS3UF5_38860; -.
DR PATRIC; fig|1111068.3.peg.3778; -.
DR HOGENOM; CLU_020120_0_2_9; -.
DR Proteomes; UP000005636; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AEV21184.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..392
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 406 AA; 43745 MW; 371CA47ECF0B4512 CRC64;
MGYYDDHYEP YEQTRRKRRS GSFVSALVGA VLGGLLVLMS IPALSRWDIL PYDVVPNQRA
EEEPKTEENG TPPIRQSVSV DVTTAVTKAI DQVSDAVVGV VNIQEASFWS QGGEAGVGSG
VIYKKAGGRA FIVTNHHVVE NASQLEVSLK DGTRVPAKLL GSDVLMDLAV LEIDAKHVKK
VAQFGNSDTV KPGEPVIAIG NPLGLQFAGS VTQGIISGTN RTVEVDLDQD GAPDWNAEVL
QTDAAINPGN SGGALVNIKG QVIGINSMKI AQEAVEGIGF AIPINTAIPI ISDLEKYGQV
RRPYMGVELR SLSDIPSYHL QATLHLPPNV TEGAAVIQVV PMSPAAQAGL KQFDVIVALD
GEKIRNVLDL RKYLYTKKSI GDRMEVTFYR DGKKRTVTMK LARESY
//