D1A4G7 · ECCC_THECD

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).

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.

113151002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Binding site479-486ATP 1 (UniProtKB | ChEBI)
Active site593
Binding site834-839ATP 2 (UniProtKB | ChEBI)
Binding site1031ATP 2 (UniProtKB | ChEBI)
Binding site1119-1124ATP 3 (UniProtKB | ChEBI)
Binding site1293ATP 3 (UniProtKB | ChEBI)
Binding site1310-1311ATP 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    ESX secretion system protein EccC
  • Alternative names
    • Type VII secretion system protein EccC
      (T7SS protein EccC
      )

Gene names

    • Name
      eccC
    • Ordered locus names
      Tcur_0607

Organism names

Accessions

  • Primary accession
    D1A4G7

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-40Cytoplasmic
Transmembrane41-61Helical
Topological domain62-64Extracellular
Transmembrane65-85Helical
Topological domain86-1315Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis543Increased intrinsic ATPase activity; ATPase is activated by wild-type but not mutant EsxBA-98.
Mutagenesis593No longer activates ATPase; when associated with A-543.
Mutagenesis616Increased intrinsic ATPase activity without concentration-dependency; when associated with A-543.
Mutagenesis892No change in intrinsic ATPase activity.
Mutagenesis1163No longer interacts with EsxB.
Mutagenesis1179No longer interacts with EsxB.
Mutagenesis1208No longer interacts with EsxB.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004383091-1315ESX secretion system protein EccC

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).

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-16Basic and acidic residues
Region1-21Disordered
Domain456-656FtsK 1
Region721-1315Binds EsxB
Domain813-1004FtsK 2
Domain1099-1282FtsK 3

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,315
  • Mass (Da)
    145,547
  • Last updated
    2010-01-19 v1
  • Checksum
    F2C5AC3BFCCB68DE
MSTVLVRRKERRQPPQMPRGEILLESPPELPEVVTNSFQNVLMYLPMAAGSAAMVFTFLNHRNTLQLVAGGMFALSMFGMMFGQLSQQSGERKTKLNSARRDYLRYLGQVRQRVRKAAKQQREALEWNNPAPGRLWSMVMSPRLWERRSSDADFAQVRIGAGPQRLAVQLIPPETKPVEDLEPMSAGALRRFLRAHSTVPDLPVAISLRSFARILPDGDPKAVYGMVRALIMQLAAFHSPDDVRITVCASRERMPQWQWMKWLPHSLHPTEYDAAGQVRLLTHSLVELESMLGPEIKDRGMFGASRAPAEPFHLVIVDGGQASYDSQIASDGIDGVCVIDLTGSVAETNEATMLRLRVTPERVYVVKRDRAGKEVLSSVGRPDQASIAEAEALARQLAPFRTSAADEPEEDVLSANMTLTSLLHIDNPYNLDPAVLWRPRPQRNRLRVPIGLDADGRPLELDIKESAQGGMGPHGLCIGATGSGKSELLRTLVLALAMTHSPEVLNFVLVDFKGGATFLGMEGLRHVSAIITNLEEELPLVDRMYDALHGEMVRRQEHLRHSGNYASLRDYEKARMEGAPLPPMPTLFIVLDEFSELLSAKPDFAELFVMIGRLGRSLGVHLLLASQRLEEGKLRGLDTHLSYRIGLRTFSAMESRVVLGVPDAYELPPSPGNGYLKFATEPLVRFKAAYVSGPVDEEPQTRSEGPQIVRQVLPYLTDYIRPQVVEQPQPEQRAEENKSSESLFDVVVRQLAGHGPEPHQIWLPPLDVPPTLDELLPPLSPSAAHGYTADGWEWRGRLHAVVGLVDRPFDQRRDPYWLDLSGGAGHVGVAGGPQTGKSTMLRTLITSLALLHTPQEVQFYCLDFGGGTLAGLAELPHVGSVATRLDADRIRRTVAEVSALLEQREQEFTERGIDSMATYRRLRATGEYAGDGFGDVFLVVDNWLTLRQDYEALEDSITQLAARGLGYGIHVVLSSNKWSEFRTSIRDLLGTKLELRLGDPYESEVDRKKAANVPENRPGRGLTRDGYHFLTALPRIDGDTSAETLTEGIATTVKTIREAWHGPTAPPVRMLPNVLPAAQLPSAAESGTRIPIGIDEDSLSPVYLDFNTDPHFLVFGDTECGKSNLLRLITAGIIERYTPQQARLIFIDYSRSLLDVATTEHQIGYAASSTAASSLVRDIKGAMEARLPPPDLTPEQLRSRSWWTGAELFLVVDDYEMVATSDNPLRPLAELLPQARDIGLHLIIARSMGGAGRALYEPIIQRIKEMASPGLVMSGNKDEGILLGNVKPHKLPQGRGYFVERRSGTRLIQTAYRES

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-16Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001738
EMBL· GenBank· DDBJ
ACY96202.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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