P45745

PR
Gene name
dhbF (BSU31960)
Protein name
Dimodular nonribosomal peptide synthase
Names
Glycine--[glycyl-carrier protein] ligase, L-threonine--[L-threonyl-carrier protein] ligase
Species
Bacillus subtilis (strain 168)
KEGG Pathway
bsu:BSU31960
EC number
6.2.1.66: Acid--thiol ligases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

2080-2149 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P45745

Entry ID Method Resolution Chain Position Source
AF-P45745-F1 Predicted AlphaFoldDB

No variants for P45745

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P45745

No associated diseases with P45745

16 regional properties for P45745

Type Name Position InterPro Accession
domain AMP-dependent synthetase/ligase domain 464 - 861 IPR000873-1
domain AMP-dependent synthetase/ligase domain 1520 - 1935 IPR000873-2
domain Thioesterase 2130 - 2280 IPR001031
domain Condensation domain 8 - 443 IPR001242-1
domain Condensation domain 1050 - 1500 IPR001242-2
domain Phosphopantetheine binding ACP domain 961 - 1036 IPR009081-1
domain Phosphopantetheine binding ACP domain 2036 - 2111 IPR009081-2
domain Amino acid adenylation domain 486 - 885 IPR010071-1
domain Amino acid adenylation domain 1541 - 1959 IPR010071-2
domain Polyketide synthase, thioesterase domain 2132 - 2369 IPR020802
domain Polyketide synthase, phosphopantetheine-binding domain 967 - 1036 IPR020806-1
domain Polyketide synthase, phosphopantetheine-binding domain 2042 - 2111 IPR020806-2
conserved_site AMP-binding, conserved site 609 - 620 IPR020845-1
conserved_site AMP-binding, conserved site 1670 - 1681 IPR020845-2
domain AMP-binding enzyme, C-terminal domain 869 - 942 IPR025110-1
domain AMP-binding enzyme, C-terminal domain 1943 - 2017 IPR025110-2

Functions

Description
EC Number 6.2.1.66 Acid--thiol ligases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
ligase activity Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
phosphopantetheine binding Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).

3 GO annotations of biological process

Name Definition
amide biosynthetic process The chemical reactions and pathways resulting in the formation of an amide, any derivative of an oxoacid in which an acidic hydroxy group has been replaced by an amino or substituted amino group.
organonitrogen compound biosynthetic process The chemical reactions and pathways resulting in the formation of organonitrogen compound.
secondary metabolite biosynthetic process The chemical reactions and pathways resulting in the formation of secondary metabolites, the compounds that are not necessarily required for growth and maintenance of cells, and are often unique to a taxon.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPDTKDLQYS LTGAQTGIWF AQQLDPDNPI YNTAEYIEIN GPVNIALFEE ALRHVIKEAE
70 80 90 100 110 120
SLHVRFGENM DGPWQMINPS PDVQLHVIDV SSEPDPEKTA LNWMKADLAK PVDLGYAPLF
130 140 150 160 170 180
NEALFIAGPD RFFWYQRIHH IAIDGFGFSL IAQRVASTYT ALIKGQTAKS RSFGSLQAIL
190 200 210 220 230 240
EEDTDYRGSE QYEKDRQFWL DRFADAPEVV SLADRAPRTS NSFLRHTAYL PPSDVNALKE
250 260 270 280 290 300
AARYFSGSWH EVMIAVSAVY VHRMTGSEDV VLGLPMMGRI GSASLNVPAM VMNLLPLRLT
310 320 330 340 350 360
VSSSMSFSEL IQQISREIRS IRRHHKYRHE ELRRDLKLIG ENHRLFGPQI NLMPFDYGLD
370 380 390 400 410 420
FAGVRGTTHN LSAGPVDDLS INVYDRTDGS GLRIDVDANP EVYSESDIKL HQQRILQLLQ
430 440 450 460 470 480
TASAGEDMLI GQMELLLPEE KEKVISKWNE TAKSEKLVSL QDMFEKQAVL TPERIALMCD
490 500 510 520 530 540
DIQVNYRKLN EEANRLARLL IEKGIGPEQF VALALPRSPE MVASMLGVLK TGAAYLPLDP
550 560 570 580 590 600
EFPADRISYM LEDAKPSCII TTEEIAASLP DDLAVPELVL DQAVTQEIIK RYSPENQDVS
610 620 630 640 650 660
VSLDHPAYII YTSGSTGRPK GVVVTQKSLS NFLLSMQEAF SLGEEDRLLA VTTVAFDISA
670 680 690 700 710 720
LELYLPLISG AQIVIAKKET IREPQALAQM IENFDINIMQ ATPTLWHALV TSEPEKLRGL
730 740 750 760 770 780
RVLVGGEALP SGLLQELQDL HCSVTNLYGP TETTIWSAAA FLEEGLKGVP PIGKPIWNTQ
790 800 810 820 830 840
VYVLDNGLQP VPPGVVGELY IAGTGLARGY FHRPDLTAER FVADPYGPPG TRMYRTGDQA
850 860 870 880 890 900
RWRADGSLDY IGRADHQIKI RGFRIELGEI DAVLANHPHI EQAAVVVRED QPGDKRLAAY
910 920 930 940 950 960
VVADAAIDTA ELRRYMGASL PDYMVPSAFV EMDELPLTPN GKLDRKALPA PDFSTSVSDR
970 980 990 1000 1010 1020
APRTPQEEIL CDLFAEVLGL ARVGIDDSFF ELGGHSLLAA RLMSRIREVM GAELGIAKLF
1030 1040 1050 1060 1070 1080
DEPTVAGLAA HLDLAQSACP ALQRAERPEK IPLSFAQRRL WFLHCLEGPS PTYNIPVAVR
1090 1100 1110 1120 1130 1140
LSGELDQGLL KAALYDLVCR HESLRTIFPE SQGTSYQHIL DADRACPELH VTEIAEKELS
1150 1160 1170 1180 1190 1200
DRLAEAVRYS FDLAAEPAFR AELFVIGPDE YVLLLLVHHI VGDGWSLTPL TRDLGTAYAA
1210 1220 1230 1240 1250 1260
RCHGRSPEWA PLAVQYADYA LWQQELLGNE DDPNSLIAGQ LAFWKETLKN LPDQLELPTD
1270 1280 1290 1300 1310 1320
YSRPAEPSHD GDTIHFRIEP EFHKRLQELA RANRVSLFMV LQSGLAALLT RLGAGTDIPI
1330 1340 1350 1360 1370 1380
GSPIAGRNDD ALGDLVGLFI NTLVLRTDTS GDPSFRELLD RVREVNLAAY DNQDLPFERL
1390 1400 1410 1420 1430 1440
VEVLNPARSR ATHPLFQIML AFQNTPDAEL HLPDMESSLR INSVGSAKFD LTLEISEDRL
1450 1460 1470 1480 1490 1500
ADGTPNGMEG LLEYSTDLFK RETAQALADR LMRLLEAAES DPDEQIGNLD ILAPEEHSSM
1510 1520 1530 1540 1550 1560
VTDWQSVSEK IPHACLPEQF EKQAALRPDA IAVVYENQEL SYAELNERAN RLARMMISEG
1570 1580 1590 1600 1610 1620
VGPEQFVALA LPRSLEMAVG LLAVLKAGAA YLPLDPDYPA DRIAFMLKDA QPAFIMTNTK
1630 1640 1650 1660 1670 1680
AANHIPPVEN VPKIVLDDPE LAEKLNTYPA GNPKNKDRTQ PLSPLNTAYV IYTSGSTGVP
1690 1700 1710 1720 1730 1740
KGVMIPHQNV TRLFAATEHW FRFSSGDIWT MFHSYAFDFS VWEIWGPLLH GGRLVIVPHH
1750 1760 1770 1780 1790 1800
VSRSPEAFLR LLVKEGVTVL NQTPSAFYQF MQAEREQPDL GQALSLRYVI FGGEALELSR
1810 1820 1830 1840 1850 1860
LEDWYNRHPE NRPQLINMYG ITETTVHVSY IELDRSMAAL RANSLIGCGI PDLGVYVLDE
1870 1880 1890 1900 1910 1920
RLQPVPPGVA GELYVSGAGL ARGYLGRPGL TSERFIADPF GPPGTRMYRT GDVARLRADG
1930 1940 1950 1960 1970 1980
SLDYVGRADH QVKIRGFRIE LGEIEAALVQ HPQLEDAAVI VREDQPGDKR LAAYVIPSEE
1990 2000 2010 2020 2030 2040
TFDTAELRRY AAERLPDYMV PAAFVTMKEL PLTPNGKLDR KALPAPDFAA AVTGRGPRTP
2050 2060 2070 2080 2090 2100
QEEILCDLFM EVLHLPRVGI DDRFFDLGGH SLLAVQLMSR IREALGVELS IGNLFEAPTV
2110 2120 2130 2140 2150 2160
AGLAERLEMG SSQSALDVLL PLRTSGDKPP LFCVHPAGGL SWCYAGLMTN IGTDYPIYGL
2170 2180 2190 2200 2210 2220
QARGIGQREE LPKTLDDMAA DYIKQIRTVQ PKGPYHLLGW SLGGNVVQAM ATQLQNQGEE
2230 2240 2250 2260 2270 2280
VSLLVMLDAY PNHFLPIKEA PDDEEALIAL LALGGYDPDS LGEKPLDFEA AIEILRRDGS
2290 2300 2310 2320 2330 2340
ALASLDETVI LNLKNTYVNS VGILGSYKPK TFRGNVLFFR STIIPEWFDP IEPDSWKPYI
2350 2360 2370
NGQIEQIDID CRHKDLCQPE PLAQIGKVLA VKLEELNK