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Database: UniProt
Entry: A0A132MPM8_9ACTN
LinkDB: A0A132MPM8_9ACTN
Original site: A0A132MPM8_9ACTN 
ID   A0A132MPM8_9ACTN        Unreviewed;       538 AA.
AC   A0A132MPM8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-FEB-2018, entry version 11.
DE   SubName: Full=Alkaline serine exoprotease A {ECO:0000313|EMBL:KWW99817.1};
GN   ORFNames=LI90_1456 {ECO:0000313|EMBL:KWW99817.1};
OS   Streptomyces thermoautotrophicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99817.1, ECO:0000313|Proteomes:UP000070188};
RN   [1] {ECO:0000313|EMBL:KWW99817.1, ECO:0000313|Proteomes:UP000070188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H1 {ECO:0000313|EMBL:KWW99817.1,
RC   ECO:0000313|Proteomes:UP000070188};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C.,
RA   Murray J.W., Woodward J., Friesen M., Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome
RT   sequences of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KWW99817.1}.
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DR   EMBL; LAXD01000001; KWW99817.1; -; Genomic_DNA.
DR   EnsemblBacteria; KWW99817; KWW99817; LI90_1456.
DR   PATRIC; fig|1469144.10.peg.1598; -.
DR   Proteomes; UP000070188; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 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; 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   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000070188};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355};
KW   Protease {ECO:0000256|RuleBase:RU003355, ECO:0000313|EMBL:KWW99817.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070188};
KW   Serine protease {ECO:0000256|RuleBase:RU003355};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     36       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        37    538       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007452654.
FT   DOMAIN      416    538       P/Homo B. {ECO:0000259|PROSITE:PS51829}.
SQ   SEQUENCE   538 AA;  55951 MW;  B55906BDEB4B02DA CRC64;
     MASTHRRARA ALRTALSVLS LTMALAGFAL TGPAAAAPTP EGKILRAGSP HAIKNSYIVV
     LDSAVLDGAR VVVSEIAKDL AGRYHGTLRR TYSAALRGFA VTMNEQQARR LAADPRIAYV
     EQDQAVRLAE TQTPTSSWGL DRIDQRNLPL NNAYTYSTTA SNVHAYVIDT GIRVSHSDFG
     GRAHLAYDSV GDGQNGNDCH GHGTHAAGIL GGSVYGVAKG VQLYAVRVLD CQGAGSISDV
     IAGVDWVTQN AKKPAVTNMS LGGGASSSLD NAVKNSIASG ITYAIAAGNG DFLGNPQDAC
     TVSPARTPEA ITVGATDSSD RRASFSNYGT CVDIFAPGVD ITSAWGDSDT ATNTVSGTSM
     ASPHVAGAAA LYLAAHPSAT PQQVHDTLVD NATSGVIQDP GDGSPNRLLY VGGGGADPPP
     PPPADYFENT TDMPIPDAGP ARYSSITVTG LSGNAPATLK IGVDIKHTYR GDLVIDLVSP
     DGSTYRLKNS SPFDRADNVI TTYTVNASSD PANGVWKLKV RDLYRGDTGY LDAWNLTF
//
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