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Database: UniProt
Entry: D5SLK0_STRCL
LinkDB: D5SLK0_STRCL
Original site: D5SLK0_STRCL 
ID   D5SLK0_STRCL            Unreviewed;       887 AA.
AC   D5SLK0;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:EFG04793.2};
GN   ORFNames=SCLAV_p1307 {ECO:0000313|EMBL:EFG04793.2};
OS   Streptomyces clavuligerus.
OG   Plasmid pSCL4 {ECO:0000313|EMBL:EFG04793.2,
OG   ECO:0000313|Proteomes:UP000002357}.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG04793.2, ECO:0000313|Proteomes:UP000002357};
RN   [1] {ECO:0000313|EMBL:EFG04793.2, ECO:0000313|Proteomes:UP000002357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC   NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RC   PLASMID=pSCL4 {ECO:0000313|EMBL:EFG04793.2};
RX   PubMed=20624727; DOI=10.1093/gbe/evq013;
RA   Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA   Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA   Breitling R., Takano E.;
RT   "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT   evolutionary reservoir of secondary metabolic pathways.";
RL   Genome Biol. Evol. 2:212-224(2010).
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DR   EMBL; CM000914; EFG04793.2; -; Genomic_DNA.
DR   RefSeq; WP_003963616.1; NZ_WKJU01000565.1.
DR   AlphaFoldDB; D5SLK0; -.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 2472181at2; -.
DR   Proteomes; UP000002357; Plasmid pSCL4.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd12117; A_NRPS_Srf_like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:EFG04793.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT   DOMAIN          799..874
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   887 AA;  88341 MW;  98EC6E8EBFAF0BAB CRC64;
     MTSTVLTSDE SQGPTGTPGP TGIPGFRGVP GFSGSGLPPF DARSIHELVA EQAERAPDAP
     AVSCGGQTLS YRQLVDRADR LARRLRDAGL RPEEVVGVLV RRSPELVVAL LAVLTAGGAY
     LGLDPEDPPA RHELLLGDAG VGMVITEEAL RERVPDGVAA VGEEGPVPVV RPVRASPAPG
     PGPDRLAYVS YTSGSTGEPK GVAVPHRAVD RLVRGADWME VRPGDVFFHI APVAFDASTL
     EIWAPLVNGC RLAVFPPGTI ALAEVARTVR AEGVTVLLLT TGLFHRMAGS HPEAFAGVRH
     VLTGGDVASP SHVERLLTLH PGLVYTNGYG PTENTTYTTC WTSDTLTNRE RVPIGGPISG
     TRIAVLDSEL RPVPAGECGE LYAAGAGLAR GYLNRPGATA ERFLPDPSGT EPGARMYRTG
     DLVRWTPDGT LEFVGRADQQ VKVQGYRAEP QAVEAALERL PGVRHAAVLP QPDPAGGTRL
     LAYVVPDGVE LAAAGGATGG GVPAGAGGGA VGTDLSADAG GGAADVDVRD GAPGGGTGGG
     VSVGARGGAA GAGVPGVSAP GGASGTVLPD GAGGGAADGD VPDGAPGEAT GGGVPAAEGG
     AAGAGVPGAS APGGAVGTVL PDGALGRAGG GGVPGGARGG AAGAGVPGDV RGRATGGDVS
     GDARGGGTGT DLPDGARERT VGRDLSADAG GTAAAGVLLA GTGSVAAQER TAAPGGATGT
     GTDLPGGGPR GGTDVMSSDV LGLGGRLRRE LRAELPAYLI PWAILVRSEL PLNRNGKVDR
     RALPGATRVP RNVPNAFTAP RTPTELRLAE LWGELLGVEP VGTDDDFFDL GGHSLLATEL
     LAAVEREFGT AVPAQTLYLS PTVAELATAL DTRLHAAAEA AAEGSTR
//
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