ID A9DRQ3_9FLAO Unreviewed; 1204 AA.
AC A9DRQ3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:EDP96827.1};
GN ORFNames=KAOT1_16728 {ECO:0000313|EMBL:EDP96827.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP96827.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP96827.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP96827.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(2011).
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:EDP96827.1}.
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DR EMBL; ABIB01000003; EDP96827.1; -; Genomic_DNA.
DR RefSeq; WP_007095881.1; NZ_DS544873.1.
DR AlphaFoldDB; A9DRQ3; -.
DR STRING; 391587.KAOT1_16728; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_003748_0_0_10; -.
DR OrthoDB; 9792152at2; -.
DR Proteomes; UP000002945; 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; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR026444; Secre_tail.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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:UP000002945};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1204
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002736758"
FT DOMAIN 242..501
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1127..1203
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 447
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1204 AA; 129324 MW; 789904DCEBDA0D23 CRC64;
MKKITQVKSL LGSLIPLLVV AIFLNCNIAQ AQSTVYFQDE VITMPNNIAS FNWNSMPENA
KFNNGYFGWA HFSETPTQAI QDQFAERNLK LIEYFPDQTY LFYAPANTNI SFLQQSGVVS
IIPIENNFKK SAQIKLNNID SYAMQGNNVL IMLQHYDFIS KDYVVEQLAS MSSVTIKENY
KTSSMLQIVI PYGQIDALVS QPFVKWVELV PAPAIKEDTR GRSLHRASNL DSQTPSGRNY
TGAGVGVMVR DDGIVGPHID FQGRIDNSSS STVGQTHGDG VAGIMAGAGN LDPTKRGMAA
GSDIYVTQYA ATFLDDATTS RINDGSVQIT NSSYGDGCND GYTVISRTVD TQTINTPALL
HVFSAGNSGT SNCGYGAGAG WGNITGGHKQ GKNVIATANT FFNGSLASSS SRGPAADGRI
KPDITAHGQN QESTAENNTY QTFGGTSGAA PGIAGVSAQL YEAYASLNGG AFPESGLIKA
TLLNTANDYG NTGPDFSFGW GMVNGLRAAM LIEDGRYLDA TISQGGNNNH SITVPANTRE
VRFMVYWTDA AAAPGASPAL VNDLDLVVTD PGSTTHQPWV LDTTPSAAFL NSPATTGADH
LNNMEQVAIT NPTAGTYNIN VAGFNVPMGP QKYYVVYEII TDGITLTYPT GGEKFVAGTQ
EVIHWDANNA VNSYVLEYST DNGATWNSMA TLPPASTNYT WNVPNGLASG QCKIRITNGT
LTDESDDNFS IASRVTGVNI SMVCPTEVTV SWNGIPSATS YDVYLLGDKF MEVAGTSTTN
SLAVPITDAF APIWVAVVAK GGNGWETLRT NAINYTGSGL FNCPLAKDLS VTAINNTAGD
FQTICNTDPI IVSAELQNDG TDPQSNFTVS YQVGSEPVVQ ETYTGTIASG TSDTFNFATP
ITLTANGDNT LRVWTSLSGD EFTNNDEQTF DFFAVVNGTA IDYSEPFDVN GVLPTGWILD
NPDNSRTWQA RANLLGIDGN TTTAAFVDGA NYTTRGQEDT MTTEYFDLNF NGTAELTFDL
AKAQWSNSFN DGLRVEISID CGATYTQVYF KDGLDLATVP NTSAAWAPSS VNDWRTEIID
ITPYVGENIL VRIININDYS NSTFVDNITL TKTLSVGENA LDKAIALYPN PAKSNVDVII
NTNIGNTYEI ELMNSIGQTI SKIEETRFSA RAQQRLDVSQ YGTGLYFVKI KVGDQVVTKK
LIVN
//
