ID A0A081PG47_9SPHI Unreviewed; 534 AA.
AC A0A081PG47;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KEQ29670.1};
GN ORFNames=N180_19690 {ECO:0000313|EMBL:KEQ29670.1};
OS Pedobacter antarcticus 4BY.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ29670.1, ECO:0000313|Proteomes:UP000028007};
RN [1] {ECO:0000313|EMBL:KEQ29670.1, ECO:0000313|Proteomes:UP000028007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4BY {ECO:0000313|EMBL:KEQ29670.1,
RC ECO:0000313|Proteomes:UP000028007};
RA Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA Reddy G., Bhargava P.M.;
RT "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT Soils of Schirmacher Oasis, Antarctica.";
RL Int. J. Syst. Bacteriol. 42:102-106(1992).
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:KEQ29670.1}.
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DR EMBL; JNFF01000066; KEQ29670.1; -; Genomic_DNA.
DR RefSeq; WP_037441553.1; NZ_JNFF01000066.1.
DR AlphaFoldDB; A0A081PG47; -.
DR eggNOG; COG1404; Bacteria.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000028007; 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:UP000028007};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..534
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001761768"
FT DOMAIN 65..492
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 287
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 456
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 534 AA; 58573 MW; 8770D57C7DEEFADC CRC64;
MNTRQNKLMM RAALSTVFAF GLGFSAFAQQ NNNWQNQDLK QDTVFGISTE KAYKELLKGK
KAVPVIVGVL DGGVETTHED LKSVIWTNKK EVAGNGKDDD KNGYIDDVHG WNFLGSAKGS
VDHETLELTR ILRRDSAKFD KQTAQTVKAE DLPAFEAYQK AKTDFDKQKD EAENAVANIS
ALKGVLDEMV KKMGKDNPDQ ADFKNVQTQT GMEDRLKGIM VSQLENTTYK DFYESQIKKG
LDHYQKQLAY NLNMNYDPRP ELVGDNYADS KERFYGNNDV AGPDASHGTH VSGIIAADRT
NNLGIKGVAD HVQIMGVRSV PDGDERDKDV ANAIRYAVEN GAKVLNMSFG KAYSWDKKAV
DDAVKYAMSK DVLIIQAAGN DNKNLDVEKS FPDRRYEGGG IADAYIVVGA SGPKDDKTLK
ASFSNYGKTT VDVFAPGVQI YSTVPGSKYE AYNGTSMASP VVAGLASLIR SYYPKLKAAQ
VKEIIMKTVT KVNHDVEISG EEGEEAKVMP FAELSISGGI VNAYEALKLA ASYK
//
