ID B5H6E7_STRE2 Unreviewed; 399 AA.
AC B5H6E7;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Alkaline serine protease {ECO:0000313|EMBL:EDY62408.2};
GN ORFNames=SSDG_00726 {ECO:0000313|EMBL:EDY62408.2};
OS Streptomyces pristinaespiralis (strain ATCC 25486 / DSM 40338 / CBS 914.69
OS / JCM 4507 / NBRC 13074 / NRRL 2958 / 5647).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457429 {ECO:0000313|EMBL:EDY62408.2, ECO:0000313|Proteomes:UP000002805};
RN [1] {ECO:0000313|Proteomes:UP000002805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 /
RC NRRL 2958 / 5647 {ECO:0000313|Proteomes:UP000002805};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 /
RC NRRL 2958 / 5647 {ECO:0000313|Proteomes:UP000002805};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces pristinaespiralis strain ATCC 25486.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CM000950; EDY62408.2; -; Genomic_DNA.
DR RefSeq; WP_005310291.1; NZ_CM000950.1.
DR AlphaFoldDB; B5H6E7; -.
DR MEROPS; S08.051; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_1_7_11; -.
DR Proteomes; UP000002805; 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; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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:UP000002805};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..399
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005664984"
FT DOMAIN 66..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 151..380
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 399 AA; 40625 MW; 7ACED0DB0B150049 CRC64;
MATHKRASRI KLTAAITAVA AAAGVTLLNT SFAGAAAPAE GKIYGANAEG AVAGSYIVML
DEKADKKGLA KEYGGELQRN YSSAINGFSA SGLTETEAKR LAADPAVAKV VQNKKFTINA
TQDNPPSWGL DRVDQADTAG DSKYNYPDSA GEGVTAYVID TGVRISHKDF EGRATHGFDA
VDNDDSADDG NGHGTHVAGT IAGAAHGVAK KAKIVAVRVL DDNGSGTTEQ VVAGIDWVTQ
NHQGPSVANM SLGGGADEAL DEAVRKAIAA GVTFGVAAGN ESSDAAQGSP SRVKEAITVA
SSTKEDAQSD FSNFGEIVDI YAPGSDITSS WNDSDEGTKT ISGTSMATPH VVGAAAVYLA
GHQDATPEQV ATALTEGATA DKITNPSTGT PNKLLKVVE
//
