ID A0A1Q3TSB1_9CHLR Unreviewed; 791 AA.
AC A0A1Q3TSB1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=BGO39_33635 {ECO:0000313|EMBL:OJW05349.1};
OS Chloroflexi bacterium 54-19.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJW05349.1, ECO:0000313|Proteomes:UP000186384};
RN [1] {ECO:0000313|EMBL:OJW05349.1, ECO:0000313|Proteomes:UP000186384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54-19 {ECO:0000313|EMBL:OJW05349.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJW05349.1}.
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DR EMBL; MKTJ01000012; OJW05349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3TSB1; -.
DR STRING; 1895928.BGO39_33635; -.
DR Proteomes; UP000186384; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
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; 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}.
FT DOMAIN 458..571
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 484..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 523
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 791 AA; 83859 MW; 74AE61803DB6B9E4 CRC64;
MAARPGYAGL DNSLYKGQPG RFTRLGCLLA LLATLLLAAC GDPSPTPAPT PSTLVQDSSK
IDTALRDLLV SYQSGGIEAA RNYAKDTGLL DGQDRVRFGL ILTGPAAAPA ITGQVQKMGG
EVYSSADEQL AVAVDLGKLT AYFNPSDKRN FLQELASFKE VKELKLLLAP PLAGPALAPP
VAPNAALNQG VALIGADRWQ KAGFNGQNIR VGIIDGGFAG YRGYLGGALP PASQVQLESY
LPGNSEGSEN HGVAVAEIVH SLAPQANLIL APIEDEIGFS RAVQFFIDKK VQIIQISLGW
GGIFPGDGTG KMDEMLDKAR QAGILPVVST GNYGQSHYMA TFNPDANGFE QFGSNKITLK
LSAEATSAWV SLRWEEPWNA PQTNLDLYLL DSAQRPVASS RNEQGEGFSK PPTELAPFRA
QPGQTYYIQV KWANPAKSLP SANLRFHLFA YNATLEESTA ESSLATPADA RGALSVGATN
WQNDKLEPYS SRGPTLDNRA KPDLVGPSDV NGSVFNQPFE GTSASAPQVS GAAALVWSAA
PEMTADQVAS YLQRNAFDLG AAGPDPLYGF GRVKLGSEEA AREGLPGLLG PVANGAPFSD
DFSAADSGLP NNKLAFYATP GATGQGYRVV ARPGELNWNS YLGHSFEEFR ASVTIQPEAI
SPALFYGLIF WQQGPDDYYT WLVSQQRYAV FKHSGSSWTA LSDWSQEAAL PVSGPVSLSL
EATTGYLRLS LGGKIIQTLT FKSGTNLAPP GQLGGKFGFG AGLFGLEQTP ANENDPVVTF
QNLLITPLST R
//
