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Database: UniProt
Entry: D9X5Y0_STRVT
LinkDB: D9X5Y0_STRVT
Original site: D9X5Y0_STRVT 
ID   D9X5Y0_STRVT            Unreviewed;       481 AA.
AC   D9X5Y0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Acyl-CoA synthase {ECO:0000313|EMBL:EFL36111.1};
GN   ORFNames=SSQG_06629 {ECO:0000313|EMBL:EFL36111.1};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL36111.1, ECO:0000313|Proteomes:UP000004184};
RN   [1] {ECO:0000313|Proteomes:UP000004184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC   {ECO:0000313|Proteomes:UP000004184};
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   "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG657757; EFL36111.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9X5Y0; -.
DR   STRING; 591159.SSQG_06629; -.
DR   eggNOG; COG0657; Bacteria.
DR   HOGENOM; CLU_046855_0_0_11; -.
DR   Proteomes; UP000004184; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..47
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           48..481
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003131865"
FT   DOMAIN          125..181
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  51148 MW;  00D1FD1069EDB930 CRC64;
     MAPARDPHGR PGLPRRHPHS GRNPALRIRL ALLTTCLSLA TALPAQAADA TDSHLEGKLP
     SGAAYVMDVP ASWNGTVLLY SHGYTPAGAP NPAQNTPGTA ARDKLLARGY ALIGSSYATN
     GWAVTEAVPD QLATLDLFTE KFGSARRTLA WGTSYGGFVT SMLAERHADR FDGSLSMCGL
     VQGGVANWNS TLDPVFALRT LLAPGSGVRL AGFADQTEAV AASKTLSSKV EAAQRTPDGR
     ARIALAAALH NIPGYNDSAQ TEPGPTDWAT QQSNQYAAVR GLLQLPAFSW RQEAESRAGG
     NPSWNTGVDY TAMLARSPLY KEVTELYKEA GLSLRTDLSA LGRAPRVSAD PQAVRWMRNT
     SVLSGRLTDP QLNIHTTGDA LIPVQAENAY HRAATGAGSA GLLRQAYVEG PGHCTFTTGE
     TLAALHTLEK RLDTGRWDVR PGTLNATAAT EDPAAEPRYI PYRPTAYPRP YDLAHPGDAR
     P
//
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