ID B1VNQ0_STRGG Unreviewed; 1114 AA.
AC B1VNQ0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Putative secreted peptidase {ECO:0000313|EMBL:BAG17073.1};
GN OrderedLocusNames=SGR_244 {ECO:0000313|EMBL:BAG17073.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17073.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG17073.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AP009493; BAG17073.1; -; Genomic_DNA.
DR RefSeq; WP_012377643.1; NC_010572.1.
DR AlphaFoldDB; B1VNQ0; -.
DR MEROPS; S08.069; -.
DR GeneID; 6214039; -.
DR KEGG; sgr:SGR_244; -.
DR PATRIC; fig|455632.4.peg.223; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_007528_0_0_11; -.
DR Proteomes; UP000001685; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
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; 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; IPR017297; Peptidase_S8A_DPH-A.
DR InterPro; IPR034213; S8_Vpr-like.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF037854; Dihydropyridine_esterase; 1.
DR PRINTS; PR00723; SUBTILISIN.
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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1114
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002769572"
FT DOMAIN 234..494
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 24..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 448
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1114 AA; 114436 MW; 1AB24B6F0DC0763E CRC64;
MRKRSTRAYA LIAAASVALS AGMTGPASGK TGGPDTASPS AAKASEAAGR TAGTVTLITG
DRVLVDAKGR VGGIERAKGR EDIPFFTEIH DGRTHVVPRD ARQLIADGRL DRRLFDITAL
ARPESLKAHR AGLKVIVGYR GASAGSARAE VRSTDGTTVR RTLSALDADA VTTAAATDDE
GALWDTLTRQ RANGSAATAS GIARIWLDGV RKASLDSSTG RIGAPAAWAR SLDGTGVKIA
VVDTGIDATH PDLAGRVAAE RNFSASPDAR DRDGHGTHVA STAAGTGAKD ARFKGVAPGA
ELINAKVLDD QGVGDDSSII AGVDWAVAQG ADVINMSLGG LDTPGIDPLE AQVNKVSAEK
GVLFAIAAGN NGPDRGTVAS PGSADAALTV GAVDDDDLIA DFSSVGPRTG DKAVKPDITA
PGVSITAAAA EGVAGQNPPG YHSLNGTSMA TPHVAGAAAI LKQKNPDWTG AQLKAALTGS
AEGGSHSVFQ QGAGRLAVDK AIDQTVVAEP VSLNLGTQAW PHTDDAPVTE QVTYRNHGSA
DVTLDLSLSA PTGGDGQPAP AGFFTLGAQR VTVPAGGTAA VDLTADTRLG GTVDGSYSAT
VVASGGGLGV RTAATVEREA ESYEVTFNAT GRDGAPSTGW QADLKGYSGH ASGQRFFPDL
SSGSVTVRLP RGTYNLSADM LVDPAAPGEG ADLINNPRFS VTGPTTVDLD ARTTRPVTFK
VPDATATPTR AGMMYALNTP ETGIVLWSDF TSFDNVRTAY QGSPVTGDST LYQQWSAHWK
RGATEYNALA GRIVPELATG YSKTYTTKNM ALVKVRIGAS APGLDGVVKA YGELANGGVD
PAFTAHPLPG TRKVYLSTDD DAVWNISAGV LGEPDPAGGR RIEAAYSWDA SRRLEPGTTH
TETFHAGVMG PRIKAGDGLV RDGDNLYGSL DLLSDGQGHT GFARYAGATT TIHRDGVLYA
KEDAAVDQGA FALPPESAAY KVATTVNRNP AVYRAGNRID ASWTFTSART EAPQTLPVST
VRFQPRLALD STVPAGSQQT FPVVVQGAAA GAGLKSLRVT VSYDGEKWLP AKVVSGKVTV
SAPAKDRAIS LRAVVTDQGG NESAVTIHNA FFGR
//
