ID A0A3D8V967_9GAMM Unreviewed; 699 AA.
AC A0A3D8V967;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:RDY65895.1};
GN ORFNames=DX912_15615 {ECO:0000313|EMBL:RDY65895.1};
OS Lysobacter soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=453783 {ECO:0000313|EMBL:RDY65895.1, ECO:0000313|Proteomes:UP000256829};
RN [1] {ECO:0000313|EMBL:RDY65895.1, ECO:0000313|Proteomes:UP000256829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22011 {ECO:0000313|EMBL:RDY65895.1,
RC ECO:0000313|Proteomes:UP000256829};
RA Zhang X., Feng G., Zhu H.;
RT "Lysobacter soli KCTC 22011, whole genome shotgun sequence.";
RL Submitted (AUG-2018) 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:RDY65895.1}.
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DR EMBL; QTJR01000013; RDY65895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8V967; -.
DR Proteomes; UP000256829; 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; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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; IPR034176; Peptidases_S8_13.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 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}; Reference proteome {ECO:0000313|Proteomes:UP000256829};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..699
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017709038"
FT DOMAIN 585..699
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 204..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 411
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 699 AA; 70833 MW; FDB53976CF4AF820 CRC64;
MSSNDRRRNR GLRAHALSIA TAIALSSALA APALAQQARV NLSGLDAQAG SDRFIVKYKD
GSAERANVST LQSALSSAAR TAGAGKALGV RHVRRIATGA DVVRADRKLD RVEAESLMRQ
IAADPNVEYV EVDKLNKPYL TPNDTRYSEQ WGYSGTYGIK ANQAWDVTNG AGSVVAVLDT
GITSHSDLSA NVLPGYDFII DTTVSNDGNG RDSDPSDPGD WVSANQCGGS HAAQPSSWHG
THVAGTIAAV TNNAKGVAGV AYGAKIVPVR VLGTCGGYDS DIADAIIWAS GGTVSGVPAN
ANPAEVINLS LGGSGACGTT TQTAINGAVS RGTTLVIAAG NDNTNVSNAS PANCNNVIAV
ASITSTGARS SFSNYGSLID IAAPGSNILS TLNSGSTTPG AETYASYNGT SMATPHVAGV
VALLQAAATT PKTPAQVESI IKANVTPFPS TPSQSIGPGI LNAKAVVDAA NGTTPPPTGT
LTNGTPVTGL SGSAGTELRY TLAVPAGATG LKFVTSGGSG DADLFVKFGS APTTTSYDCK
SEGSTNAETC NIATAQAGTY HVLVRGYSTF SGLSLTGSYT AGGGGGTQTY SNATDYTISD
NATVDSPITV SGRTGNAPTN ASVTVAIVHT YQGDLKVDLV APDGSLYNVH NRTGGSADNV
NKTVTFNLST EPLNGTWKLR VNDNAAGDTG YINSWSVTF
//