ID A0A0R2X4W0_9FLAO Unreviewed; 570 AA.
AC A0A0R2X4W0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KRP28654.1};
GN ORFNames=ABS28_05720 {ECO:0000313|EMBL:KRP28654.1};
OS Cryomorphaceae bacterium BACL22 MAG-120619-bin32.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655630 {ECO:0000313|EMBL:KRP28654.1, ECO:0000313|Proteomes:UP000052139};
RN [1] {ECO:0000313|EMBL:KRP28654.1, ECO:0000313|Proteomes:UP000052139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL3 MAG-120619-bin32 {ECO:0000313|EMBL:KRP28654.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRP28654.1}.
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DR EMBL; LIDG01000113; KRP28654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2X4W0; -.
DR Proteomes; UP000052139; 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; cd07483; Peptidases_S8_Subtilisin_Novo-like; 1.
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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034080; Protease_P7-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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 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..570
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006427624"
FT DOMAIN 82..519
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 89
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 316
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 486
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 570 AA; 63561 MW; 76624155520FC77D CRC64;
MRILKSIFLS AFAALFLASC ASTQKVLSLP NFDAPIKITP KQSVLSEEEE KFWSHADLTK
DSIAGMSLEK AYQFLEGKKP TSVIVAIADS GVDIEHEDLK DVLWMNTKEI KGNNIDDDKN
GYVDDIYGWN FLGNASGKII NADQLEITRL VKKRREKFGD KKSEEIAEND TYEFESYQRL
NQEYMLTISQ KEFEIQEMQQ TISNLERVKQ VFTDVKKLVG KEKLRLSDLD SLKPTSLMMI
SQIEAIKKIL ENGSNEDDLL EYYQKVADYT KELKKAIKGY DLDLNVRETL GDDLYDINDK
FYGNNNVIGD KDLEKHGTHV AGIVAASRIN NKGAKGVANT VKTMTVRIVP DGDEHDKDVA
LGIRYAVDNG AKIINTSFGK RFSPNKEWVF DAIEYAAKKD VLIVNAAGND GKDIDIRETY
PNDSKDLKTE FADNVITIGA SGLYYNEELV ASFSNYGKIN VDIFAPGVDI YSTVPKNEYE
PLSGTSMAAP STSGVAALIR AYYPALTAKQ VKYILMNSGV KIDFKVIKPG SQTGENPEGE
LVPFADLSVS GRIVNAYNAL QLADYLSRKK
//
