ID D7C5Q1_STRBB Unreviewed; 980 AA.
AC D7C5Q1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase {ECO:0000313|EMBL:ADI12430.1};
GN OrderedLocusNames=SBI_09312 {ECO:0000313|EMBL:ADI12430.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI12430.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI12430.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI12430.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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; CP002047; ADI12430.1; -; Genomic_DNA.
DR RefSeq; WP_014181877.1; NC_016582.1.
DR AlphaFoldDB; D7C5Q1; -.
DR STRING; 749414.SBI_09312; -.
DR KEGG; sbh:SBI_09312; -.
DR PATRIC; fig|749414.3.peg.9593; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR HOGENOM; CLU_000022_2_13_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
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; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 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 Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT DOMAIN 635..710
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 423..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 105794 MW; 1BF40A34CF173A14 CRC64;
MLSFQNNTRA TLDLPGLDIA HQPLGGIAAR FDLTVNLSEL RAGDGSPGGL SGHVDYRTDL
FDAASMEALA GRLVRVLESV TADPDLPVSR IDVLGDAERH QVLTVWNDTA HPLPDTLLPE
LFEAQVARTP DAVAVVFEGH KVSYSELNRR VNRLARYLIG QGAGPEHLVA VALPRSAELV
ITLLAILKTG AGYLPIDPDY PTDRIHYMLQ DATPTLLVTD TTTSPTLPHI HNLPHIQLDA
PDTRTAITTQ TSTDITDTDR TAGLLGQHPA YVIYTSGSTG HPKGVVIPHQ ALLNYVARCP
HAYPSLTGAT VLHASVSFDA GVTVLYGALI CGGRVHITTL TPTPGDGDGP TPGDTPVTFM
KLTPSHLPLL EHTTLQPTGQ LMLGGEAVPT EAVHTWQTHH PHTPVINHYG PTETTVGATD
HPIPPPTTTT PTTTTHTTGT VPIGRPMWNT HTYILDHTLQ PTPTGTPGEL YIAGTQLARG
YLNHPTLTAQ RFIPNPYGPP GTRMYRTGDL ARWNTNGTLH YLGRTDTQIK IRGFRIEPGE
IEAALTTHHT ITQAAVLVRE DQPGDKRLTA YAVPADAEAG IDTAQVLRTL RDQLPDYMVP
TTLITLDHLP LTPNGKLNHK ALPTPHHTPT TTQRPPRTPH EKTLTQLFTE TLGITQIGID
DNFFTLGGHS LLATRLISRI RTALDVELTI RALFEAPTVA GLAERIEDGT SQDPFDPLLP
IRSSGDEPPL FCVHPVSGLS WCYAGLLRHI PEEVPIYGLQ SRGLMGKEPL PTSLEEMARD
YVKLMRSVQP VGPYRLLGWS FGGLVAHAAA VLLQSQGEVV SLLSMLDAYP NDGVIPSGPE
KEEDLIYALA EGAGYKIPED ADAADLSALL RDYARQHMGY MTGGIALSED EISALAVAVG
NNRALGRSAA LEKFSGDVLF FTAAVDNHMP VAAPRAWAPY ITGHVHEHPV PCEHVNMMQP
GPLAEIGRTL AAALRERPEQ
//
