D1A4G7 · ECCC_THECD
- ProteinESX secretion system protein EccC
- GeneeccC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1315 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (PubMed:25865481).
Has weak intrinsic ATPase activity; probably only the first FtsK domain can hydrolyze ATP (PubMed:25865481).
Might be the translocase subunit (PubMed:25865481).
Has weak intrinsic ATPase activity; probably only the first FtsK domain can hydrolyze ATP (PubMed:25865481).
Might be the translocase subunit (PubMed:25865481).
Miscellaneous
Unlike the well characterized M.tuberculosis ESX-1 cluster, this protein is not split into 2 genes. This subunit and a WGX100 family protein are the only proteins universally associated with T7SS.
Activity regulation
EsxB binding to the third FtsK domain causes multimerization; a subsequent unknown step relieves the allosteric inhibition of linker 2 on FtsK domain 1, activating the ATPase activity; a mutant EsxB ('Ala-98') does not cause multimers to form (PubMed:25865481).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 479-486 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: GATGSGKS | ||||||
Active site | 593 | |||||
Sequence: E | ||||||
Binding site | 834-839 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: QTGKST | ||||||
Binding site | 1031 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 1119-1124 | ATP 3 (UniProtKB | ChEBI) | ||||
Sequence: ECGKSN | ||||||
Binding site | 1293 | ATP 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 1310-1311 | ATP 3 (UniProtKB | ChEBI) | ||||
Sequence: TA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameESX secretion system protein EccC
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Thermomonosporaceae > Thermomonospora
Accessions
- Primary accessionD1A4G7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-40 | Cytoplasmic | ||||
Sequence: MSTVLVRRKERRQPPQMPRGEILLESPPELPEVVTNSFQN | ||||||
Transmembrane | 41-61 | Helical | ||||
Sequence: VLMYLPMAAGSAAMVFTFLNH | ||||||
Topological domain | 62-64 | Extracellular | ||||
Sequence: RNT | ||||||
Transmembrane | 65-85 | Helical | ||||
Sequence: LQLVAGGMFALSMFGMMFGQL | ||||||
Topological domain | 86-1315 | Cytoplasmic | ||||
Sequence: SQQSGERKTKLNSARRDYLRYLGQVRQRVRKAAKQQREALEWNNPAPGRLWSMVMSPRLWERRSSDADFAQVRIGAGPQRLAVQLIPPETKPVEDLEPMSAGALRRFLRAHSTVPDLPVAISLRSFARILPDGDPKAVYGMVRALIMQLAAFHSPDDVRITVCASRERMPQWQWMKWLPHSLHPTEYDAAGQVRLLTHSLVELESMLGPEIKDRGMFGASRAPAEPFHLVIVDGGQASYDSQIASDGIDGVCVIDLTGSVAETNEATMLRLRVTPERVYVVKRDRAGKEVLSSVGRPDQASIAEAEALARQLAPFRTSAADEPEEDVLSANMTLTSLLHIDNPYNLDPAVLWRPRPQRNRLRVPIGLDADGRPLELDIKESAQGGMGPHGLCIGATGSGKSELLRTLVLALAMTHSPEVLNFVLVDFKGGATFLGMEGLRHVSAIITNLEEELPLVDRMYDALHGEMVRRQEHLRHSGNYASLRDYEKARMEGAPLPPMPTLFIVLDEFSELLSAKPDFAELFVMIGRLGRSLGVHLLLASQRLEEGKLRGLDTHLSYRIGLRTFSAMESRVVLGVPDAYELPPSPGNGYLKFATEPLVRFKAAYVSGPVDEEPQTRSEGPQIVRQVLPYLTDYIRPQVVEQPQPEQRAEENKSSESLFDVVVRQLAGHGPEPHQIWLPPLDVPPTLDELLPPLSPSAAHGYTADGWEWRGRLHAVVGLVDRPFDQRRDPYWLDLSGGAGHVGVAGGPQTGKSTMLRTLITSLALLHTPQEVQFYCLDFGGGTLAGLAELPHVGSVATRLDADRIRRTVAEVSALLEQREQEFTERGIDSMATYRRLRATGEYAGDGFGDVFLVVDNWLTLRQDYEALEDSITQLAARGLGYGIHVVLSSNKWSEFRTSIRDLLGTKLELRLGDPYESEVDRKKAANVPENRPGRGLTRDGYHFLTALPRIDGDTSAETLTEGIATTVKTIREAWHGPTAPPVRMLPNVLPAAQLPSAAESGTRIPIGIDEDSLSPVYLDFNTDPHFLVFGDTECGKSNLLRLITAGIIERYTPQQARLIFIDYSRSLLDVATTEHQIGYAASSTAASSLVRDIKGAMEARLPPPDLTPEQLRSRSWWTGAELFLVVDDYEMVATSDNPLRPLAELLPQARDIGLHLIIARSMGGAGRALYEPIIQRIKEMASPGLVMSGNKDEGILLGNVKPHKLPQGRGYFVERRSGTRLIQTAYRES |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 543 | Increased intrinsic ATPase activity; ATPase is activated by wild-type but not mutant EsxBA-98. | ||||
Sequence: R → A | ||||||
Mutagenesis | 593 | No longer activates ATPase; when associated with A-543. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 616 | Increased intrinsic ATPase activity without concentration-dependency; when associated with A-543. | ||||
Sequence: R → Q | ||||||
Mutagenesis | 892 | No change in intrinsic ATPase activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 1163 | No longer interacts with EsxB. | ||||
Sequence: I → T | ||||||
Mutagenesis | 1179 | No longer interacts with EsxB. | ||||
Sequence: I → N | ||||||
Mutagenesis | 1208 | No longer interacts with EsxB. | ||||
Sequence: L → T |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000438309 | 1-1315 | ESX secretion system protein EccC | |||
Sequence: MSTVLVRRKERRQPPQMPRGEILLESPPELPEVVTNSFQNVLMYLPMAAGSAAMVFTFLNHRNTLQLVAGGMFALSMFGMMFGQLSQQSGERKTKLNSARRDYLRYLGQVRQRVRKAAKQQREALEWNNPAPGRLWSMVMSPRLWERRSSDADFAQVRIGAGPQRLAVQLIPPETKPVEDLEPMSAGALRRFLRAHSTVPDLPVAISLRSFARILPDGDPKAVYGMVRALIMQLAAFHSPDDVRITVCASRERMPQWQWMKWLPHSLHPTEYDAAGQVRLLTHSLVELESMLGPEIKDRGMFGASRAPAEPFHLVIVDGGQASYDSQIASDGIDGVCVIDLTGSVAETNEATMLRLRVTPERVYVVKRDRAGKEVLSSVGRPDQASIAEAEALARQLAPFRTSAADEPEEDVLSANMTLTSLLHIDNPYNLDPAVLWRPRPQRNRLRVPIGLDADGRPLELDIKESAQGGMGPHGLCIGATGSGKSELLRTLVLALAMTHSPEVLNFVLVDFKGGATFLGMEGLRHVSAIITNLEEELPLVDRMYDALHGEMVRRQEHLRHSGNYASLRDYEKARMEGAPLPPMPTLFIVLDEFSELLSAKPDFAELFVMIGRLGRSLGVHLLLASQRLEEGKLRGLDTHLSYRIGLRTFSAMESRVVLGVPDAYELPPSPGNGYLKFATEPLVRFKAAYVSGPVDEEPQTRSEGPQIVRQVLPYLTDYIRPQVVEQPQPEQRAEENKSSESLFDVVVRQLAGHGPEPHQIWLPPLDVPPTLDELLPPLSPSAAHGYTADGWEWRGRLHAVVGLVDRPFDQRRDPYWLDLSGGAGHVGVAGGPQTGKSTMLRTLITSLALLHTPQEVQFYCLDFGGGTLAGLAELPHVGSVATRLDADRIRRTVAEVSALLEQREQEFTERGIDSMATYRRLRATGEYAGDGFGDVFLVVDNWLTLRQDYEALEDSITQLAARGLGYGIHVVLSSNKWSEFRTSIRDLLGTKLELRLGDPYESEVDRKKAANVPENRPGRGLTRDGYHFLTALPRIDGDTSAETLTEGIATTVKTIREAWHGPTAPPVRMLPNVLPAAQLPSAAESGTRIPIGIDEDSLSPVYLDFNTDPHFLVFGDTECGKSNLLRLITAGIIERYTPQQARLIFIDYSRSLLDVATTEHQIGYAASSTAASSLVRDIKGAMEARLPPPDLTPEQLRSRSWWTGAELFLVVDDYEMVATSDNPLRPLAELLPQARDIGLHLIIARSMGGAGRALYEPIIQRIKEMASPGLVMSGNKDEGILLGNVKPHKLPQGRGYFVERRSGTRLIQTAYRES |
Interaction
Subunit
The cytosolic domain can form homodimers (PubMed:25865481).
Binds EsxB, which leads to multimerization, however EsxA disassembles the multimers, possibly by making EccC-EsxA-EsxB trimers instead of EccC-EsxB-EsxB-EccC tetramers. Forms a complex with EsxA and EsxB, probably wholly mediated by EsxB (PubMed:25865481).
Binds EsxB, which leads to multimerization, however EsxA disassembles the multimers, possibly by making EccC-EsxA-EsxB trimers instead of EccC-EsxB-EsxB-EccC tetramers. Forms a complex with EsxA and EsxB, probably wholly mediated by EsxB (PubMed:25865481).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Basic and acidic residues | ||||
Sequence: MSTVLVRRKERRQPPQ | ||||||
Region | 1-21 | Disordered | ||||
Sequence: MSTVLVRRKERRQPPQMPRGE | ||||||
Domain | 456-656 | FtsK 1 | ||||
Sequence: GRPLELDIKESAQGGMGPHGLCIGATGSGKSELLRTLVLALAMTHSPEVLNFVLVDFKGGATFLGMEGLRHVSAIITNLEEELPLVDRMYDALHGEMVRRQEHLRHSGNYASLRDYEKARMEGAPLPPMPTLFIVLDEFSELLSAKPDFAELFVMIGRLGRSLGVHLLLASQRLEEGKLRGLDTHLSYRIGLRTFSAMESR | ||||||
Region | 721-1315 | Binds EsxB | ||||
Sequence: RPQVVEQPQPEQRAEENKSSESLFDVVVRQLAGHGPEPHQIWLPPLDVPPTLDELLPPLSPSAAHGYTADGWEWRGRLHAVVGLVDRPFDQRRDPYWLDLSGGAGHVGVAGGPQTGKSTMLRTLITSLALLHTPQEVQFYCLDFGGGTLAGLAELPHVGSVATRLDADRIRRTVAEVSALLEQREQEFTERGIDSMATYRRLRATGEYAGDGFGDVFLVVDNWLTLRQDYEALEDSITQLAARGLGYGIHVVLSSNKWSEFRTSIRDLLGTKLELRLGDPYESEVDRKKAANVPENRPGRGLTRDGYHFLTALPRIDGDTSAETLTEGIATTVKTIREAWHGPTAPPVRMLPNVLPAAQLPSAAESGTRIPIGIDEDSLSPVYLDFNTDPHFLVFGDTECGKSNLLRLITAGIIERYTPQQARLIFIDYSRSLLDVATTEHQIGYAASSTAASSLVRDIKGAMEARLPPPDLTPEQLRSRSWWTGAELFLVVDDYEMVATSDNPLRPLAELLPQARDIGLHLIIARSMGGAGRALYEPIIQRIKEMASPGLVMSGNKDEGILLGNVKPHKLPQGRGYFVERRSGTRLIQTAYRES | ||||||
Domain | 813-1004 | FtsK 2 | ||||
Sequence: RDPYWLDLSGGAGHVGVAGGPQTGKSTMLRTLITSLALLHTPQEVQFYCLDFGGGTLAGLAELPHVGSVATRLDADRIRRTVAEVSALLEQREQEFTERGIDSMATYRRLRATGEYAGDGFGDVFLVVDNWLTLRQDYEALEDSITQLAARGLGYGIHVVLSSNKWSEFRTSIRDLLGTKLELRLGDPYESE | ||||||
Domain | 1099-1282 | FtsK 3 | ||||
Sequence: LSPVYLDFNTDPHFLVFGDTECGKSNLLRLITAGIIERYTPQQARLIFIDYSRSLLDVATTEHQIGYAASSTAASSLVRDIKGAMEARLPPPDLTPEQLRSRSWWTGAELFLVVDDYEMVATSDNPLRPLAELLPQARDIGLHLIIARSMGGAGRALYEPIIQRIKEMASPGLVMSGNKDEGIL |
Domain
The cytoplasmic domain is a rigid structure with 4 domains (residues 276 to 401 form an unnamed domain) plus the 3 FtsK (ATPase) domains which are connected by short linkers. Binds EsxB via a small pocket (residues 1163-1208) in the third FtsK (ATPase) domain; the linkers between FtsK 1-2 and FtsK 2-3 bind in an analogous manner to FtsK 1 and FtsK 2. Linker 2 binding to FtsK 1 decreases its ATPase activity and probably controls it (PubMed:25865481).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,315
- Mass (Da)145,547
- Last updated2010-01-19 v1
- ChecksumF2C5AC3BFCCB68DE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Basic and acidic residues | ||||
Sequence: MSTVLVRRKERRQPPQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001738 EMBL· GenBank· DDBJ | ACY96202.1 EMBL· GenBank· DDBJ | Genomic DNA |