ID F2RGA4_STRVP Unreviewed; 600 AA.
AC F2RGA4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Extracellular protease {ECO:0000313|EMBL:CCA59824.1};
GN OrderedLocusNames=SVEN_6538 {ECO:0000313|EMBL:CCA59824.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA59824.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA59824.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR845719; CCA59824.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RGA4; -.
DR STRING; 953739.SVEN_6538; -.
DR KEGG; sve:SVEN_6538; -.
DR PATRIC; fig|953739.5.peg.1756; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4935; Bacteria.
DR HOGENOM; CLU_011263_8_2_11; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; 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; IPR034176; Peptidases_S8_13.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 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; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 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:UP000006854};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..600
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003285302"
FT DOMAIN 482..600
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 230
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 420
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 600 AA; 60281 MW; 0F63BFD18B7F4AFB CRC64;
MVASAAILGA AATTGAFAAA PGAATPKPAP ASQTMRALPS APVEKVIVTY KSQATEAGSN
TAAKNDTAEK AAKTGEKLSF ERRLAGGGAL VDLGDSATKQ DVAEVMDAFR ADPSVASVEP
DIRAYAMAVT PNDTDYAKQW DLFEPTGGMN VPSAWDKTTG SGVTVAVIDT GYAAHTDVAA
NVVNGYDFIS TSADARDGNG RDADAKDEGD WNATAGECGV GSTASNSSWH GTHVAGTIGA
VTNNAKGIAG IAYNAKIQPV RVLGKCGGSS SDIADAITWA SGGTVPGVPA NPTPAKVINM
SLGGASATCP SVYQNAINGA VSRGTTVVVA AGNSNANASG FTPANCANVI NVASTSREGN
RSYYSNFGSI VDVSAPGGET RRATDTPGTV TTPENGIYST LNSGTTVQSA ENYKPYQGTS
MAAPHIAGLA ALLKSAKSTL TPAEIESAIK ANARPLPGTC TGGCGTGIAD SAKTVDAVTG
TTTPPTGTVF TNATDVTIAD NATVSSSIAV TGRTGNAPAA LKVGVDIKHT WRGDLVIDLV
APDGTVRNLK ASSSSDSADD VVTTYTVDAS SEVANGTWKL QVRDVASGDT GYINSWSLTF
//
