ID A4X0X4_SALTO Unreviewed; 519 AA.
AC A4X0X4;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:ABP52524.1};
GN OrderedLocusNames=Strop_0039 {ECO:0000313|EMBL:ABP52524.1};
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS 105044 / CNB-440).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP52524.1, ECO:0000313|Proteomes:UP000000235};
RN [1] {ECO:0000313|Proteomes:UP000000235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC {ECO:0000313|Proteomes:UP000000235};
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP000667; ABP52524.1; -; Genomic_DNA.
DR RefSeq; WP_011903961.1; NC_009380.1.
DR AlphaFoldDB; A4X0X4; -.
DR STRING; 369723.Strop_0039; -.
DR MEROPS; S08.051; -.
DR KEGG; stp:Strop_0039; -.
DR PATRIC; fig|369723.5.peg.39; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_011263_1_7_11; -.
DR Proteomes; UP000000235; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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:UP000000235};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..519
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002676305"
FT DOMAIN 397..519
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 375..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 519 AA; 53208 MW; 9B2C07A2A10D3238 CRC64;
MGLSRRSVFV GLATMAMVAS ATPAMAAEPV GEIRSAGGAT AVTDSYIVVF KDNVVSRATV
ETSVDRLVDR HGGQVSRTYS TALRGAELRV DAGAAARIAA DPAVAYVEQN HRVSITDTQT
NPPSWGLDRV DQRDLPLDNS YTYPNTASDV NIYILDTGIR TTHQDFGGRA TWGTNTADNN
DTDCNGHGTH VAGTAAGTAH GIAKEANLVA VKVLDCAGNG TFAGVVAGVD WVTANAVQPA
VANMSLGGGA NSALDNAVSN SIDSGVTYAL AAGNSSANAC NYSPARTPDA ITVGSTTSTD
GLSWFSNIGT CLDIFAPGSS ITAPWITSDT STNTISGTSM ASPHVAGAAA LVLSANPSYT
PQQIRDELVD NATDGAIGSP GSGSPNKLLY VGDGGTTPPP PPPPGCSGTN DTDVAIPDAG
SAVTSSITIA GCDRDAAATS TVAVDIPHTW RGDLVIDLIA PDGSSYRLKT NNLSDSADNV
NETYTVNLSS EAADGTWQLQ VRDVYRQDTG YIDTWTLTV
//
