ID A0A0J5GWD2_9BACI Unreviewed; 809 AA.
AC A0A0J5GWD2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KMJ58984.1};
GN ORFNames=AB685_07880 {ECO:0000313|EMBL:KMJ58984.1};
OS Bacillus sp. LL01.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1665556 {ECO:0000313|EMBL:KMJ58984.1, ECO:0000313|Proteomes:UP000036436};
RN [1] {ECO:0000313|EMBL:KMJ58984.1, ECO:0000313|Proteomes:UP000036436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMJ58984.1,
RC ECO:0000313|Proteomes:UP000036436};
RA Vilo C., Galetovic A., Araya J., Gomez Silva B., Dong Q.;
RT "Draft Genome Sequence of a Bacillus Bacterium from the Atacama Desert
RT Wetlands Metagenome.";
RL Submitted (JUN-2015) 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}.
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:KMJ58984.1}.
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DR EMBL; LFEL01000002; KMJ58984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J5GWD2; -.
DR PATRIC; fig|1665556.3.peg.2558; -.
DR Proteomes; UP000036436; 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 CDD; cd02133; PA_C5a_like; 1.
DR CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
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; IPR034213; S8_Vpr-like.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
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 Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..809
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039124573"
FT DOMAIN 55..139
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 172..583
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 388..457
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 206..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 530
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 809 AA; 86327 MW; 00AF115B2968D0C8 CRC64;
MKQKLIAAFM PLLVLVLVFS TFATNGVSAN TGKENLELAT LQGEFDLSSS KAVKVIVELQ
EQSIVEAKHN GKKQSKQNLK SARDKVKKEV AERTSKSKVE REYDYVFSGF SLEIKANEIP
SLLATPGIKA VYPNVEYTTT EELVPAEAYS PAMADSAPFI GSNDAWDLGF TGKGVKVAII
DTGVDYTHPD LAPNFGEYLG WDFVDNDADP QETPKGDPRG AETTHGSHVA GTVAANGQIK
GVAPDATLLA YRVLGPGGSG STENVVAAIE RAVQDGADVM NLSLGNSLNA PDWATSIALD
QAMAEGVVAV TSNGNSGPNN WTVGSPGTSR EAISVGATQL PYNVYNASIF TSEGVEYPSA
KVQGFPSDDA LTNLDGNEYE FVYVGLGYPQ DFEGKDLEGK IALIIRGEIP FVDKATAAKN
AGAVGAIIYN NVAGEMPEVP GMDVPTIMLT NADGLKLQEE LASGNNTVSF NIDFNQTVGE
TMAGFSSRGP VVDTWMIKPD VSAPGVNIVS TVPTFNPDAP HGYGAKQGTS MAAPHVAGAA
AVILQANPDW DVYEVKSALM NTAEKIIDPA TGEEYAHNSQ GAGSIRVVDA LQAETLVNPG
SYSFGIFDKK KGKQVERQQF EIQNLSNKAK KYNMEFSFKN EVGKHVKVTT SKNLRVNPGK
TQKVNVNVQV DASKLEPGYY EGHLVVTEGD TEIQVPTILF VGEPDYPRVT HFGFTPLGAN
NFEFYSYLPG GAEELEVWVY TATAAGGLGT YVGDALYDAD LGKGYNYHDW NGSLVDGSHL
PAGDYRIAVY AKKGNLDRAI LATDVLKIN
//
