ID D6AGT0_STRFL Unreviewed; 851 AA.
AC D6AGT0;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:EFE79032.2};
GN ORFNames=SSGG_06399 {ECO:0000313|EMBL:EFE79032.2};
OS Streptomyces filamentosus NRRL 15998.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE79032.2, ECO:0000313|Proteomes:UP000003986};
RN [1] {ECO:0000313|Proteomes:UP000003986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RA Molnar K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces roseosporus strain NRRL 15998.";
RL Submitted (DEC-2008) 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; DS999644; EFE79032.2; -; Genomic_DNA.
DR RefSeq; WP_006129019.1; NZ_DS999644.1.
DR AlphaFoldDB; D6AGT0; -.
DR Proteomes; UP000003986; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43806:SF59; EXTRACELLULAR PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF13620; CarboxypepD_reg; 2.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
DR PROSITE; PS51318; TAT; 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..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..851
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003081091"
FT DOMAIN 190..437
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 247
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 417
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 851 AA; 87547 MW; 92C8CA0E111B223A CRC64;
MHLSRSPRRR AAAWAAAAAL TAAGLLIGPP PAAAGTGPSA RVDAALLDAV DGGGEASFFV
VLKDRADLSA ARSKRAHAAR TKSAFTELRA EADSSQRALN SFLDRKKVGH QNFWIANAVK
VTGDEALVKE LAGRSDVARI VKEQHYTLDD VEARPAEAAA AEGTDADATP EWGIKDIKAD
QVWKDYDNRG EGVVIANIDS GVQYDHPDLV TNYRGNNGDG SFTHDYNWYD PTGQCGTGGT
PCDNNGHGTH TMGTMAGRGG VGVAPNATWI AAKGCETSSC SDESLLKAGQ WILAPTDRAG
QNPRPDLAPN IVNNSWGGGA TTFYQDIVEA WNAAGIFEAF AAGNKGDGRT CGTTEAPGAQ
APAYGVGAYD ADGRIAGFSG FGPSPVDGSA KPNISAPGVD VRSTWPGSAY KALNGTSMAT
PHVAGAVALL WSAAPSLIGD IAGTRALLDE GALDVDDTHC GGTPGRNNVW GEGKLDIFAS
LDKAPHTAVD VSGKVTDEAT GAALPGVTVR ATTGAATRSV TTGADGSYRL SLPPGTYTFS
LSGYGYGTGT VSGVELITGE PVTRDVALTP VAAHAVTGTV LDVTGKPLAK AAVSLPGTPV
EEATTDAKGR FSLPKVAEGA YTLRVTPAAP VLCNGTYSGT LDVDGAEATE VKLPNRTDAG
GTYSCAPVTP SWIKGSTGTG LTGDEDATTV YLPFPVRFYG VTYTSASVTT NGLINFVQPR
LGDYANTALP ADARPNGVVA AFWDDLVLDK RSSVKTAVTG KAGARKFAIV WDKASFAAEP
SVRISFQAVF DEATGAITLQ YRGAGSSVLQ RGGSATTGIE NQAGTDGLGH SFDEAVLSDT
TALHFTPKDA R
//