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sslE sslE btuB btuB tatB tatB tatA tatA hdeB hdeB argD argD secG secG tolC tolC bamD bamD bamB bamB fadL fadL ompC ompC cirA cirA fliK fliK fliC fliC slyB slyB ompW ompW pliG pliG fhuE fhuE flgL flgL flgK flgK flgG flgG flgF flgF flgE flgE flgD flgD flgC flgC flgB flgB ompA ompA ompF ompF ompX ompX ybgF ybgF pal pal tatE tatE fepA fepA ompT ompT bolA bolA tsx tsx secD secD rcsF rcsF
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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from curated databases
experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
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sslEPutative secreted and surface-associated lipoprotein mucinase; Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane. (1520 aa)
btuBVitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. (614 aa)
tatBTatABCE protein translocation system subunit; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. (171 aa)
tatATatABCE protein translocation system subunit; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. Belongs to the TatA/E family. (89 aa)
hdeBAcid-resistance protein; Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins. (108 aa)
argDBifunctional acetylornithine aminotransferase and succinyldiaminopimelate aminotransferase; Involved in both the arginine and lysine biosynthetic pathways; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (406 aa)
secGPreprotein translocase membrane subunit; Subunit of the protein translocation channel SecYEG. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY. Treatment with antibiotics that block translation elongation such as chloramphenicol also leads to degradation of SecY and SecE but not SecG. (110 aa)
tolCTransport channel; Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells. (493 aa)
bamDBamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete a [...] (245 aa)
bamBBamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...] (392 aa)
fadLLong-chain fatty acid outer membrane transporter; Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel; Belongs to the OmpP1/FadL family. (446 aa)
ompCOuter membrane porin protein C; Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (367 aa)
cirAColicin IA outer membrane receptor and translocator; Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. (663 aa)
fliKFlagellar hook-length control protein; Controls the length of the flagellar hook; Belongs to the FliK family. (375 aa)
fliCFlagellar filament structural protein (flagellin); Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (498 aa)
slyBPutative outer membrane protein; Belongs to the Pcp/SlyB lipoprotein family. (155 aa)
ompWOuter membrane protein W; Acts as a receptor for colicin S4. (212 aa)
pliGPeriplasmic inhibitor of g-type lysozyme; Inhibits activity of g-type lysozyme, which confers increased lysozyme tolerance to the bacterium. (133 aa)
fhuEFerric-rhodotorulic acid outer membrane transporter; Required for the uptake of Fe(3+) via coprogen, ferrioxamine B, and rhodotorulic acid. (729 aa)
flgLFlagellar biosynthesis; hook-filament junction protein; Protein involved in flagellum assembly, protein folding and taxis. (317 aa)
flgKFlagellar biosynthesis, hook-filament junction protein 1; Protein involved in flagellum assembly, protein folding and taxis; Belongs to the flagella basal body rod proteins family. (547 aa)
flgGFlagellar biosynthesis, cell-distal portion of basal-body rod; Protein involved in flagellum assembly and taxis. (260 aa)
flgFFlagellar biosynthesis, cell-proximal portion of basal-body rod; Protein involved in flagellum assembly and taxis. (251 aa)
flgEFlagellar biosynthesis, hook protein; Protein involved in flagellum assembly and taxis. (402 aa)
flgDFlagellar hook assembly protein; Required for flagellar hook formation. May act as a scaffolding protein. (231 aa)
flgCFlagellar biosynthesis, cell-proximal portion of basal-body rod; Protein involved in flagellum assembly and taxis. (134 aa)
flgBFlagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body (By similarity). (138 aa)
ompAOuter membrane protein A (3a;II*;G;d); With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape. Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes. A very abundant protein, there can be up to 210,000 OmpA molecules per cell. Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, whic [...] (346 aa)
ompFOuter membrane porin 1a (Ia;b;F); Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (362 aa)
ompXOuter membrane protein X; Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpX family. (171 aa)
ybgFPeriplasmic TolA-binding protein; Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division. Promotes physical and functional coordination of the PBP1B-LpoB and Tol machines, and regulates PBP1B activity in response to Tol energy state. (263 aa)
palPeptidoglycan-associated outer membrane lipoprotein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. (173 aa)
tatESec-independent protein translocase protein TatE; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatE shares overlapping functions with TatA; Belongs to the TatA/E family. TatE subfamily. (67 aa)
fepAFerrienterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D. (746 aa)
ompTDLP12 prophage; Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues. (317 aa)
bolAStationary-phase morphogene, transcriptional repressor for mreB; Transcriptional regulator that plays an important role in general stress response. Has many effects on cell morphology, cell growth and cell division. Acts by regulating the transcription of many genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably involved in the coordination of genes that adapt the cell physiology in order to enhance cell adaptation and survival under stress conditions. Essential for normal cell morphology in stationary phase and under conditions of starvation. Also regulates a complex n [...] (105 aa)
tsxNucleoside channel, receptor of phage T6 and colicin K; Functions as substrate-specific channel for nucleosides and deoxynucleosides. Has a greater affinity for deoxynucleosides than for nucleosides, and does not transport free bases. In addition, constitutes the receptor for colicin K and phage T6. Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family. (294 aa)
secDSecYEG protein translocase auxillary subunit; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. The large periplasmic domain is thought to have a base and head domain joined by a hinge; movement of the hinge may be coupled to both proton transport and protein export, with the head domain capturing substrate, and a conformational change preventing backward movement and driving forward movement. Expression of V.alginolyti [...] (615 aa)
rcsFPutative outer membrane protein; Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division. Belongs to the RcsF family. (134 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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