Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Dimodular nonribosomal peptide synthase |
Protein Synonyms/Alias | |
Gene Name | dhbF |
Gene Synonyms/Alias | BSU31960 |
Created Date | 3-June-2014 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Phosphorylation | Position | Peptide | Code | Type | References | 996 | FFELGGHSLLAARLM | S | HTP | [1],UniProt | 988 | ARVGIDDSFFELGGH | S | HTP | [1] | |
Reference | [1]The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Macek B,Mijakovic I,Olsen JV,Gnad F,Kumar C,Jensen PR,Mann M Mol. Cell Proteomics 2007, Apr;6(4):697-707. [ PMID:17218307] |
Functional Description From UniProt | FUNCTION: Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains |
| MOD_RES 996 996 O-(pantetheine 4'-phosphoryl)serine MOD_RES 2071 2071 O-(pantetheine 4'-phosphoryl)serine (Potential) |
| Completeproteome; Ligase; Phosphopantetheine; Phosphoprotein; Referenceproteome; Repeat |
Protein Sequence | MPDTKDLQYS LTGAQTGIWF AQQLDPDNPI YNTAEYIEIN GPVNIALFEE ALRHVIKEAE 60 SLHVRFGENM DGPWQMINPS PDVQLHVIDV SSEPDPEKTA LNWMKADLAK PVDLGYAPLF 120 NEALFIAGPD RFFWYQRIHH IAIDGFGFSL IAQRVASTYT ALIKGQTAKS RSFGSLQAIL 180 EEDTDYRGSE QYEKDRQFWL DRFADAPEVV SLADRAPRTS NSFLRHTAYL PPSDVNALKE 240 AARYFSGSWH EVMIAVSAVY VHRMTGSEDV VLGLPMMGRI GSASLNVPAM VMNLLPLRLT 300 VSSSMSFSEL IQQISREIRS IRRHHKYRHE ELRRDLKLIG ENHRLFGPQI NLMPFDYGLD 360 FAGVRGTTHN LSAGPVDDLS INVYDRTDGS GLRIDVDANP EVYSESDIKL HQQRILQLLQ 420 TASAGEDMLI GQMELLLPEE KEKVISKWNE TAKSEKLVSL QDMFEKQAVL TPERIALMCD 480 DIQVNYRKLN EEANRLARLL IEKGIGPEQF VALALPRSPE MVASMLGVLK TGAAYLPLDP 540 EFPADRISYM LEDAKPSCII TTEEIAASLP DDLAVPELVL DQAVTQEIIK RYSPENQDVS 600 VSLDHPAYII YTSGSTGRPK GVVVTQKSLS NFLLSMQEAF SLGEEDRLLA VTTVAFDISA 660 LELYLPLISG AQIVIAKKET IREPQALAQM IENFDINIMQ ATPTLWHALV TSEPEKLRGL 720 RVLVGGEALP SGLLQELQDL HCSVTNLYGP TETTIWSAAA FLEEGLKGVP PIGKPIWNTQ 780 VYVLDNGLQP VPPGVVGELY IAGTGLARGY FHRPDLTAER FVADPYGPPG TRMYRTGDQA 840 RWRADGSLDY IGRADHQIKI RGFRIELGEI DAVLANHPHI EQAAVVVRED QPGDKRLAAY 900 VVADAAIDTA ELRRYMGASL PDYMVPSAFV EMDELPLTPN GKLDRKALPA PDFSTSVSDR 960 APRTPQEEIL CDLFAEVLGL ARVGIDDSFF ELGGHSLLAA RLMSRIREVM GAELGIAKLF 1020 DEPTVAGLAA HLDLAQSACP ALQRAERPEK IPLSFAQRRL WFLHCLEGPS PTYNIPVAVR 1080 LSGELDQGLL KAALYDLVCR HESLRTIFPE SQGTSYQHIL DADRACPELH VTEIAEKELS 1140 DRLAEAVRYS FDLAAEPAFR AELFVIGPDE YVLLLLVHHI VGDGWSLTPL TRDLGTAYAA 1200 RCHGRSPEWA PLAVQYADYA LWQQELLGNE DDPNSLIAGQ LAFWKETLKN LPDQLELPTD 1260 YSRPAEPSHD GDTIHFRIEP EFHKRLQELA RANRVSLFMV LQSGLAALLT RLGAGTDIPI 1320 GSPIAGRNDD ALGDLVGLFI NTLVLRTDTS GDPSFRELLD RVREVNLAAY DNQDLPFERL 1380 VEVLNPARSR ATHPLFQIML AFQNTPDAEL HLPDMESSLR INSVGSAKFD LTLEISEDRL 1440 ADGTPNGMEG LLEYSTDLFK RETAQALADR LMRLLEAAES DPDEQIGNLD ILAPEEHSSM 1500 VTDWQSVSEK IPHACLPEQF EKQAALRPDA IAVVYENQEL SYAELNERAN RLARMMISEG 1560 VGPEQFVALA LPRSLEMAVG LLAVLKAGAA YLPLDPDYPA DRIAFMLKDA QPAFIMTNTK 1620 AANHIPPVEN VPKIVLDDPE LAEKLNTYPA GNPKNKDRTQ PLSPLNTAYV IYTSGSTGVP 1680 KGVMIPHQNV TRLFAATEHW FRFSSGDIWT MFHSYAFDFS VWEIWGPLLH GGRLVIVPHH 1740 VSRSPEAFLR LLVKEGVTVL NQTPSAFYQF MQAEREQPDL GQALSLRYVI FGGEALELSR 1800 LEDWYNRHPE NRPQLINMYG ITETTVHVSY IELDRSMAAL RANSLIGCGI PDLGVYVLDE 1860 RLQPVPPGVA GELYVSGAGL ARGYLGRPGL TSERFIADPF GPPGTRMYRT GDVARLRADG 1920 SLDYVGRADH QVKIRGFRIE LGEIEAALVQ HPQLEDAAVI VREDQPGDKR LAAYVIPSEE 1980 TFDTAELRRY AAERLPDYMV PAAFVTMKEL PLTPNGKLDR KALPAPDFAA AVTGRGPRTP 2040 QEEILCDLFM EVLHLPRVGI DDRFFDLGGH SLLAVQLMSR IREALGVELS IGNLFEAPTV 2100 AGLAERLEMG SSQSALDVLL PLRTSGDKPP LFCVHPAGGL SWCYAGLMTN IGTDYPIYGL 2160 QARGIGQREE LPKTLDDMAA DYIKQIRTVQ PKGPYHLLGW SLGGNVVQAM ATQLQNQGEE 2220 VSLLVMLDAY PNHFLPIKEA PDDEEALIAL LALGGYDPDS LGEKPLDFEA AIEILRRDGS 2280 ALASLDETVI LNLKNTYVNS VGILGSYKPK TFRGNVLFFR STIIPEWFDP IEPDSWKPYI 2340 NGQIEQIDID CRHKDLCQPE PLAQIGKVLA VKLEELNK 2378 |
| GO:0016788 F:hydrolase activity, acting on ester bonds IEA:InterPro GO:0016874 F:ligase activity IEA:UniProtKB-KW GO:0031177 F:phosphopantetheine binding IEA:InterPro GO:0009058 P:biosynthetic process IEA:InterPro |
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