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mhuD mhuD aroG aroG mbtA mbtA ahpC ahpC ideR ideR hupB hupB devS devS devR devR dosT dosT katG katG bfrA bfrA tlyA tlyA irtA irtA mbtK mbtK mmpS5 mmpS5 mmpL5 mmpL5 mmpS4 mmpS4 mmpL4 mmpL4 esxH esxH esxG esxG PPE4 PPE4 PE5 PE5 mmpL3 mmpL3 Rv0203 Rv0203 mmpL11 mmpL11 PPE37 PPE37 bfrB bfrB Rv3525c Rv3525c
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second shell of interactors
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proteins of unknown 3D structure
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mhuDPossible heme degrading protein MhuD; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron. (105 aa)
aroGPhospho-2-dehydro-3-deoxyheptonate aldolase AroG; Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate. (462 aa)
mbtABifunctional enzyme MbtA: salicyl-AMP ligase (SAL-AMP ligase) + salicyl-S-ArCP synthetase; Involved in the initial steps of the mycobactin biosynthetic pathway. Catalyzes the salicylation of the aryl carrier protein (ArCP) domain of MbtB through a two-step reaction. The first step is the ATP- dependent adenylation of salicylate to generate a salicyl-AMP intermediate. The second step is the transfer of this activated salicylate to MbtB to form a salicyl-ArCP domain thioester. (565 aa)
ahpCAlkyl hydroperoxide reductase C protein AhpC (alkyl hydroperoxidase C); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Together with AhpD, DlaT and Lpd, constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. D [...] (195 aa)
ideRIron-dependent repressor and activator IdeR; Metal-dependent DNA-binding protein that controls transcription of many genes involved in iron metabolism. Acts as a repressor of siderophore biosynthesis and as a positive modulator of iron storage. Also regulates expression of transporters, proteins involved in siderophore synthesis, iron storage and transcriptional regulators. (230 aa)
hupBDNA-binding protein HU homolog HupB (histone-like protein) (HLP) (21-kDa laminin-2-binding protein); Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Binds DNA non-specifically. Induces lymphoproliferation, particularly in health tuberculin reactors, and is immunogenic. Maybe involved in pathogenesis of inflammatory bowel disease (IBD) in patients with ulcerative colitis and Crohn disease (CD). Bound by anti-neutrophil cytoplasmic antibodies (pANCA), which are a hallmark of IB [...] (214 aa)
devSTwo component sensor histidine kinase DevS; Member of the two-component regulatory system DevR/DevS (DosR/DosS) involved in onset of the dormancy response. Regulates an approximately 48-member regulon. Required for full induction of the DevR (DosR) regulon; acts later than DosT to positively regulate expression of the DevR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Autophosph [...] (578 aa)
devRTwo component transcriptional regulatory protein DevR (probably LuxR/UhpA-family); Member of the two-component regulatory system DevR/DevS (also called DosR/DosS) involved in onset of the dormancy response. Regulates an approximately 48-member regulon. When phosphorylated binds and activates the promoter of DevR regulon genes in response to hypoxia. The presence of target DNA increases stability of phospho-DevR in vitro. Activates its own transcription under hypoxic but not aerobic conditions, probably binds as a dimer to tandem binding sites within the devR and hspX promoters. Accepts [...] (217 aa)
dosTTwo component sensor histidine kinase DosT; Interacts with the two-component regulatory system DevR/DevS (DosR/DosS) involved in onset of the dormancy response. Required for full induction of the DevR (DosR) regulon; required during early adaptation to anaerobiosis, to start induction of the DevR regulon. May act as a direct hypoxia/oxygen sensor. O(2) acts as a switch, with the Fe(2+)-O(2)-bound protein inactive in autophosphorylation. Autophosphorylates under anaerobic but not aerobic conditions, binding of NO or CO has no effect on autophosphorylation. Binds a number of gases; O(2), [...] (573 aa)
katGCatalase-peroxidase-peroxynitritase T KatG; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity, oxidizing various electron donors including NADP(H). Protects M.tuberculosis against toxic reactive oxygen species (ROS) including hydrogen peroxide as well as organic peroxides and thus contributes to its survival within host macrophages by countering the phagocyte oxidative burst. Also displays efficient peroxynitritase activity, which may help the bacterium to persist in macrophages. Catalyzes the oxidative activation of the antitubercular pro- drug isoniazid (I [...] (740 aa)
bfrAProbable bacterioferritin BfrA; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. (159 aa)
tlyA2'-O-methyltransferase TlyA; Acts as a host evasion factor, that significantly contributes to the pathogenesis of M.tuberculosis by modulating adaptive immune responses by inhibiting host-protective Th1 and Th17 cytokine responses as well as autophagy. Catalyzes the 2'-O-methylation at nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA. Is likely involved in ribosomal biogenesis. Also exhibits hemolytic activity in vitro, by binding with and oligomerizing into host cell membranes. Belongs to the TlyA family. (268 aa)
irtAIron-regulated transporter IrtA; Part of the ABC transporter complex IrtAB involved in iron import. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for replication in human macrophages and in mouse lungs. (859 aa)
mbtKLysine N-acetyltransferase MbtK; Acyltransferase required for the direct transfer of medium- to long-chain fatty acyl moieties from a carrier protein (MbtL) on to the epsilon-amino group of lysine residue in the mycobactin core. (210 aa)
mmpS5Possible conserved membrane protein MmpS5; Part of an export system, which is required for biosynthesis and secretion of siderophores. Essential for virulence. Belongs to the MmpS family. (142 aa)
mmpL5Probable conserved transmembrane transport protein MmpL5; Part of an export system, which is required for biosynthesis and secretion of siderophores. (964 aa)
mmpS4Probable conserved membrane protein MmpS4; Part of an export system, which is required for biosynthesis and secretion of siderophores. Essential for virulence. (140 aa)
mmpL4Probable conserved transmembrane transport protein MmpL4; Part of an export system, which is required for biosynthesis and secretion of siderophores. Essential for normal replication during the active-growth phase of the murine tuberculosis model. (967 aa)
esxHLow molecular weight protein antigen 7 EsxH (10 kDa antigen) (CFP-7) (protein TB10.4); EsxH, in complex with EsxG, disrupts ESCRT function and impairs host phagosome maturation, thereby promoting intracellular bacterial growth. The complex acts by interacting, via EsxH, with the host hepatocyte growth factor-regulated tyrosine kinase substrate (HGS/HRS), a component of the ESCRT machinery. Belongs to the WXG100 family. ESAT-6 subfamily. (96 aa)
esxGESAT-6 like protein EsxG (conserved protein TB9.8); EsxG, in complex with EsxH, disrupts ESCRT function and impairs host phagosome maturation, thereby promoting intracellular bacterial growth. The complex acts by interacting, via EsxH, with the host hepatocyte growth factor-regulated tyrosine kinase substrate (HGS/HRS), a component of the ESCRT machinery. EsxG stabilizes EsxH in the host cytosol. (97 aa)
PPE4PPE family protein PPE4; Important for the siderophore-mediated iron-acquisition function of ESX-3; Belongs to the mycobacterial PPE family. (513 aa)
PE5PE family protein PE5; Important for the siderophore-mediated iron-acquisition function of ESX-3. May play a pivotal role in the evasion of host immune response by M.tuberculosis. Mediates production of IL-10 via activation of the p38 and ERK1/2 mitogen-activated protein kinase (MAPK) signaling pathways. (102 aa)
mmpL3Possible conserved transmembrane transport protein MmpL3; Transports trehalose monomycolate (TMM) across the inner membrane. Could also be part of a heme-iron acquisition system. Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily. (944 aa)
Rv0203Possible exported protein; Part of a heme-iron acquisition system. Acts by binding heme and delivering it to the membrane proteins MmpL3 and MmpL11. Can use free heme or heme from host hemoglobin. (136 aa)
mmpL11Probable conserved transmembrane transport protein MmpL11; Part of a heme-iron acquisition system. Receives heme from the heme-binding protein Rv0203 and transports it into the mycobacterial cell. Contributes to virulence. Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily. (966 aa)
PPE37Rv2123, (MTCY261.19), len: 473 aa. PPE37 (alternate gene name: irg2), member of the Mycobacterium tuberculosis PPE family of proteins but the C-terminus is not repetitive (see citation below). (473 aa)
bfrBBacterioferritin BfrB; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex; Belongs to the ferritin family. Prokaryotic subfamily. (181 aa)
Rv3525cRv3525c, (MTCY3C7.31), len: 174 aa. Possible siderophore-binding protein, similar to ferripyochelin binding proteins (and related) e.g. Q9RSN5|DR2089 ferripyochelin-binding protein from Deinococcus radiodurans (240 aa), FASTA scores: opt: 472, E(): 3.3e-21, (46.9% identity in 162 aa overlap); O59257|PH1591 long hypothetical ferripyochelin binding protein from Pyrococcus horikoshii (173 aa), FASTA scores: opt: 431, E(): 6.7e-19,(40.0% identity in 170 aa overlap); Q9V158|FBP|PAB0393 ferripyochelin binding protein from Pyrococcus abyssi (173 aa), FASTA scores: opt: 429, E(): 8.9e-19, (39. [...] (174 aa)
Your Current Organism:
Mycobacterium tuberculosis H37Rv
NCBI taxonomy Id: 83332
Other names: M. tuberculosis H37Rv, Mycobacterium sp. H37Rv, Mycobacterium tuberculosis str. H37Rv, Mycobacterium tuberculosis strain H37Rv
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