ID A0A246A804_9SPHI Unreviewed; 586 AA.
AC A0A246A804;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:OWK68782.1};
GN ORFNames=CBW18_20105 {ECO:0000313|EMBL:OWK68782.1};
OS Pedobacter sp. AJM.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2003629 {ECO:0000313|EMBL:OWK68782.1, ECO:0000313|Proteomes:UP000198039};
RN [1] {ECO:0000313|Proteomes:UP000198039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJM {ECO:0000313|Proteomes:UP000198039};
RA Mcnett A.J., Newman J.D.;
RL Submitted (MAY-2017) 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:OWK68782.1}.
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DR EMBL; NHOT01000017; OWK68782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246A804; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000198039; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198039};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 65..546
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 73
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 510
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 586 AA; 65496 MW; C8C2774D4919DD23 CRC64;
MTNFSQRKLL TLIVFILVQM GAYAQNKNVK LPANWFNLDL AESGYFGISA EKAYRDLLKD
KKPKENIIVA VIDGGVDINH PDLKPVLWVN QKEIPGNGID DDENGYIDDI HGWNFIGSKK
GNLEFDNLEL VRLLRIYTPK YQSTTNLTPL DSNQKEEFRL YKKMVGDFGK KYEDASNTFS
VLVAINKVLD SVATINHKQI PTYEDIEKYK ADDETEEQVK TIIKKGSRED GGFDKFYKNI
KDGYKQYDAM LKYNLNPKYD KRAELVGDDY ANSQDRNYGN ADVKGPDAMH GTHVSGIIGA
DRNNNLGILG VANHVRIMAI RVVPTGDERD KDVANGIRYA VDNGARVINM SFGKAYKWDK
KVVDEAVKYA ESNGVLLVHA AGNDHQNNDV EENFPNKYYD GAEAEAYKSA HRKPLKPDFI
PQKPVGQHTM GMRPPMGIAV PKQVPLDSAK FSLPSATNWI EVGASAYKDD ETLKADFSNY
GKYNVDVFAP GFLINSTIPD GKYEELDGTS MASPVVSGLA ALILSYYPQL KPAQVREIIM
KSVSKVNRKV KYKNEKGENT RALFSEICVS GGIVNAYNAL KLAVTY
//
