ID DHBF_BACSU Reviewed; 2378 AA.
AC P45745; Q9R9I2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 4.
DT 27-NOV-2024, entry version 166.
DE RecName: Full=Dimodular nonribosomal peptide synthase {ECO:0000303|PubMed:11112781};
DE EC=6.2.1.66 {ECO:0000269|PubMed:11112781};
DE EC=6.2.1.70 {ECO:0000269|PubMed:11112781};
DE AltName: Full=Glycine--[glycyl-carrier protein] ligase {ECO:0000305};
DE AltName: Full=L-threonine--[L-threonyl-carrier protein] ligase {ECO:0000305};
GN Name=dhbF; OrderedLocusNames=BSU31960;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=168;
RX PubMed=11112781; DOI=10.1074/jbc.m009140200;
RA May J.J., Wendrich T.M., Marahiel M.A.;
RT "The dhb operon of Bacillus subtilis encodes the biosynthetic template for
RT the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric
RT ester bacillibactin.";
RL J. Biol. Chem. 276:7209-7217(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [4]
RP SEQUENCE REVISION TO 2141.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8550523; DOI=10.1128/jb.178.3.854-861.1996;
RA Rowland B.M., Taber H.W.;
RT "Duplicate isochorismate synthase genes of Bacillus subtilis: regulation
RT and involvement in the biosyntheses of menaquinone and 2,3-
RT dihydroxybenzoate.";
RL J. Bacteriol. 178:854-861(1996).
RN [6]
RP PHOSPHOPANTETHEINYLATION [LARGE SCALE ANALYSIS] AT SER-996, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
CC -!- FUNCTION: Specifically adenylates L-threonine and, to a lesser extent,
CC glycine and covalently loads both amino acids onto their corresponding
CC peptidyl carrier domains. {ECO:0000269|PubMed:11112781}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[peptidyl-carrier protein] + L-threonine + ATP = L-
CC threonyl-[peptidyl-carrier protein] + AMP + diphosphate;
CC Xref=Rhea:RHEA:61688, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15908,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144927, ChEBI:CHEBI:456215;
CC EC=6.2.1.70; Evidence={ECO:0000269|PubMed:11112781};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61689;
CC Evidence={ECO:0000269|PubMed:11112781};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[peptidyl-carrier protein] + glycine + ATP = glycyl-
CC [peptidyl-carrier protein] + AMP + diphosphate; Xref=Rhea:RHEA:61696,
CC Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15909, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:144951, ChEBI:CHEBI:456215; EC=6.2.1.66;
CC Evidence={ECO:0000269|PubMed:11112781};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61697;
CC Evidence={ECO:0000269|PubMed:11112781};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Siderophore biosynthesis; bacillibactin biosynthesis.
CC {ECO:0000305|PubMed:11112781}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: The phosphoserine observed at Ser-996 in PubMed:17218307
CC undoubtedly results from the secondary neutral loss of pantetheine from
CC the phosphodiester linked cofactor. {ECO:0000305}.
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; AF184977; AAD56240.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15186.3; -; Genomic_DNA.
DR EMBL; U26444; AAC44634.1; -; Genomic_DNA.
DR PIR; E69615; E69615.
DR RefSeq; NP_391076.3; NC_000964.3.
DR RefSeq; WP_009968094.1; NZ_OZ025638.1.
DR AlphaFoldDB; P45745; -.
DR SMR; P45745; -.
DR IntAct; P45745; 3.
DR MINT; P45745; -.
DR STRING; 224308.BSU31960; -.
DR ESTHER; bacsu-YUKL; Thioesterase.
DR jPOST; P45745; -.
DR PaxDb; 224308-BSU31960; -.
DR EnsemblBacteria; CAB15186; CAB15186; BSU_31960.
DR GeneID; 936569; -.
DR KEGG; bsu:BSU31960; -.
DR PATRIC; fig|224308.179.peg.3462; -.
DR eggNOG; COG1020; Bacteria.
DR InParanoid; P45745; -.
DR OrthoDB; 9765680at2; -.
DR PhylomeDB; P45745; -.
DR BioCyc; BSUB:BSU31960-MONOMER; -.
DR BioCyc; MetaCyc:MONOMER-13921; -.
DR BRENDA; 6.2.1.66; 658.
DR UniPathway; UPA00013; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd17643; A_NRPS_Cytc1-like; 1.
DR CDD; cd12116; A_NRPS_Ta1_like; 1.
DR CDD; cd19538; LCL_NRPS; 1.
DR CDD; cd19533; starter-C_NRPS; 1.
DR FunFam; 3.30.300.30:FF:000010; Enterobactin synthetase component F; 2.
DR FunFam; 3.40.50.980:FF:000002; Enterobactin synthetase component F; 1.
DR FunFam; 1.10.1200.10:FF:000016; Non-ribosomal peptide synthase; 1.
DR FunFam; 3.30.559.10:FF:000012; Non-ribosomal peptide synthetase; 1.
DR FunFam; 3.30.559.30:FF:000001; Non-ribosomal peptide synthetase; 1.
DR FunFam; 3.40.50.12780:FF:000012; Non-ribosomal peptide synthetase; 2.
DR FunFam; 3.40.50.980:FF:000001; Non-ribosomal peptide synthetase; 2.
DR FunFam; 2.30.38.10:FF:000001; Non-ribosomal peptide synthetase PvdI; 2.
DR FunFam; 1.10.1200.10:FF:000005; Nonribosomal peptide synthetase 1; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 4.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase_fold.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
PE 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2378
FT /note="Dimodular nonribosomal peptide synthase"
FT /id="PRO_0000193081"
FT DOMAIN 961..1036
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2036..2111
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 996
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:17218307"
FT MOD_RES 2071
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 2141
FT /note="S -> G (in Ref. 1; AAD56240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2378 AA; 263770 MW; 80216ABF9D6BFA66 CRC64;
MPDTKDLQYS LTGAQTGIWF AQQLDPDNPI YNTAEYIEIN GPVNIALFEE ALRHVIKEAE
SLHVRFGENM DGPWQMINPS PDVQLHVIDV SSEPDPEKTA LNWMKADLAK PVDLGYAPLF
NEALFIAGPD RFFWYQRIHH IAIDGFGFSL IAQRVASTYT ALIKGQTAKS RSFGSLQAIL
EEDTDYRGSE QYEKDRQFWL DRFADAPEVV SLADRAPRTS NSFLRHTAYL PPSDVNALKE
AARYFSGSWH EVMIAVSAVY VHRMTGSEDV VLGLPMMGRI GSASLNVPAM VMNLLPLRLT
VSSSMSFSEL IQQISREIRS IRRHHKYRHE ELRRDLKLIG ENHRLFGPQI NLMPFDYGLD
FAGVRGTTHN LSAGPVDDLS INVYDRTDGS GLRIDVDANP EVYSESDIKL HQQRILQLLQ
TASAGEDMLI GQMELLLPEE KEKVISKWNE TAKSEKLVSL QDMFEKQAVL TPERIALMCD
DIQVNYRKLN EEANRLARLL IEKGIGPEQF VALALPRSPE MVASMLGVLK TGAAYLPLDP
EFPADRISYM LEDAKPSCII TTEEIAASLP DDLAVPELVL DQAVTQEIIK RYSPENQDVS
VSLDHPAYII YTSGSTGRPK GVVVTQKSLS NFLLSMQEAF SLGEEDRLLA VTTVAFDISA
LELYLPLISG AQIVIAKKET IREPQALAQM IENFDINIMQ ATPTLWHALV TSEPEKLRGL
RVLVGGEALP SGLLQELQDL HCSVTNLYGP TETTIWSAAA FLEEGLKGVP PIGKPIWNTQ
VYVLDNGLQP VPPGVVGELY IAGTGLARGY FHRPDLTAER FVADPYGPPG TRMYRTGDQA
RWRADGSLDY IGRADHQIKI RGFRIELGEI DAVLANHPHI EQAAVVVRED QPGDKRLAAY
VVADAAIDTA ELRRYMGASL PDYMVPSAFV EMDELPLTPN GKLDRKALPA PDFSTSVSDR
APRTPQEEIL CDLFAEVLGL ARVGIDDSFF ELGGHSLLAA RLMSRIREVM GAELGIAKLF
DEPTVAGLAA HLDLAQSACP ALQRAERPEK IPLSFAQRRL WFLHCLEGPS PTYNIPVAVR
LSGELDQGLL KAALYDLVCR HESLRTIFPE SQGTSYQHIL DADRACPELH VTEIAEKELS
DRLAEAVRYS FDLAAEPAFR AELFVIGPDE YVLLLLVHHI VGDGWSLTPL TRDLGTAYAA
RCHGRSPEWA PLAVQYADYA LWQQELLGNE DDPNSLIAGQ LAFWKETLKN LPDQLELPTD
YSRPAEPSHD GDTIHFRIEP EFHKRLQELA RANRVSLFMV LQSGLAALLT RLGAGTDIPI
GSPIAGRNDD ALGDLVGLFI NTLVLRTDTS GDPSFRELLD RVREVNLAAY DNQDLPFERL
VEVLNPARSR ATHPLFQIML AFQNTPDAEL HLPDMESSLR INSVGSAKFD LTLEISEDRL
ADGTPNGMEG LLEYSTDLFK RETAQALADR LMRLLEAAES DPDEQIGNLD ILAPEEHSSM
VTDWQSVSEK IPHACLPEQF EKQAALRPDA IAVVYENQEL SYAELNERAN RLARMMISEG
VGPEQFVALA LPRSLEMAVG LLAVLKAGAA YLPLDPDYPA DRIAFMLKDA QPAFIMTNTK
AANHIPPVEN VPKIVLDDPE LAEKLNTYPA GNPKNKDRTQ PLSPLNTAYV IYTSGSTGVP
KGVMIPHQNV TRLFAATEHW FRFSSGDIWT MFHSYAFDFS VWEIWGPLLH GGRLVIVPHH
VSRSPEAFLR LLVKEGVTVL NQTPSAFYQF MQAEREQPDL GQALSLRYVI FGGEALELSR
LEDWYNRHPE NRPQLINMYG ITETTVHVSY IELDRSMAAL RANSLIGCGI PDLGVYVLDE
RLQPVPPGVA GELYVSGAGL ARGYLGRPGL TSERFIADPF GPPGTRMYRT GDVARLRADG
SLDYVGRADH QVKIRGFRIE LGEIEAALVQ HPQLEDAAVI VREDQPGDKR LAAYVIPSEE
TFDTAELRRY AAERLPDYMV PAAFVTMKEL PLTPNGKLDR KALPAPDFAA AVTGRGPRTP
QEEILCDLFM EVLHLPRVGI DDRFFDLGGH SLLAVQLMSR IREALGVELS IGNLFEAPTV
AGLAERLEMG SSQSALDVLL PLRTSGDKPP LFCVHPAGGL SWCYAGLMTN IGTDYPIYGL
QARGIGQREE LPKTLDDMAA DYIKQIRTVQ PKGPYHLLGW SLGGNVVQAM ATQLQNQGEE
VSLLVMLDAY PNHFLPIKEA PDDEEALIAL LALGGYDPDS LGEKPLDFEA AIEILRRDGS
ALASLDETVI LNLKNTYVNS VGILGSYKPK TFRGNVLFFR STIIPEWFDP IEPDSWKPYI
NGQIEQIDID CRHKDLCQPE PLAQIGKVLA VKLEELNK
//
