ID A0A1D8RRY5_9GAMM Unreviewed; 834 AA.
AC A0A1D8RRY5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:AOW75864.1};
GN ORFNames=A3Q34_02745 {ECO:0000313|EMBL:AOW75864.1};
OS Colwellia sp. PAMC 20917.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=1816218 {ECO:0000313|EMBL:AOW75864.1, ECO:0000313|Proteomes:UP000177820};
RN [1] {ECO:0000313|EMBL:AOW75864.1, ECO:0000313|Proteomes:UP000177820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20917 {ECO:0000313|EMBL:AOW75864.1,
RC ECO:0000313|Proteomes:UP000177820};
RA Kim H.-W.;
RT "Complete genome sequence of Colwellia sp. PAMC 20917.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP014944; AOW75864.1; -; Genomic_DNA.
DR RefSeq; WP_070373949.1; NZ_CP014944.1.
DR AlphaFoldDB; A0A1D8RRY5; -.
DR STRING; 1816218.A3Q34_02745; -.
DR KEGG; coz:A3Q34_02745; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000177820; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR001119; SLH_dom.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF00395; SLH; 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:UP000177820};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..834
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009437168"
FT DOMAIN 140..450
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 618..658
FT /note="SLH"
FT /evidence="ECO:0000259|Pfam:PF00395"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 403
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 834 AA; 89109 MW; 4635FBF5B5D1B0A5 CRC64;
MKKFTLSAIA AATMALTMPS QVFANAAIGE QLAEFLPTMV GSQTVMAVVT YNQLEPVSTT
QLEHLSGLGI SQAVQFASVP VIGVVANLDQ IKAIAQRSDV RSVWLNRELE YFNSDARQIT
GVDAVQGDEF FKQNGIEYTG KGVTVMVNDS GIDATHQDLF FGDKVIDNVQ GLTHASLLSI
TGVTEGLILK NQPNTDTNSG HGTHCAGTIA GYGTMSDGKY PGAAPDAKLV GYGSGGVILI
LDTIGAYDYA ITKGDSYENP LRVMSNSWGS SGKFDPTGPV SLASYKAHKM GILSVFAAGN
SGSGEDTHNP YAQIPWGMSI GAGEKDGTLA GFSSRGYKYE SGEFTMPGGE KWTYNNEITI
VAPGVDVIST RAVTNAGANG GEADVDAMDP THLPFYTMIS GTSMATPHVA GIVALMLEAN
PDLDNMAIKK LLQESATNMP GYERFEVGAG FVNARAAVAA AKNYDMNHSV TVNNLRGKVF
NANTLVEISE KSPEGSIWST PNGVTEPLGL QNSFDFQVHS EALWVKGSAS SLANTAKLVL
IDPDGTEYFG NLTLPVLETG MRVTAPAMAG TWTVRVDGLT SLSGVNPDPL DLTNGPMAPE
NFDVKINFED LIGFEGVSDI AAHRYENAIK YAVSKRLMDG LKNDNFNPDA KLKRKDLAKY
LVMGGAVRQY RTLDSEPEPT LNEVPSGYKA IIESVSVVGG ALKDSLRTQQ PVMLSENGEF
AHNGRVSKVD LAYSLVQILG LESMAKAFDP EKDNITVDYK GQTIVLADQD SIADNMKGYV
QLAIQLSLLN VHFDVTQGTY DLTPQLNASF GGNYKVTRAE YALTAGRLFG QYFQ
//