Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
UniProtKB entry for E. coli CcmC (P0ABM1)
-
Curated record gives inner-membrane location, six predicted transmembrane helices and CcmC/CycZ/HelC family membership.
"Belongs to the CcmC/CycZ/HelC family."
Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB.
-
CcmC is the only Ccm protein strictly required for heme attachment to CcmE, and is sufficient for it when overexpressed.
"it is the only Ccm protein that is strictly required for heme transfer and attachment to CcmE"
-
Conserved histidines H60 and H184 are required for CcmC function.
"Both H60 and H184 of CcmC were found to be required for the incorporation of heme into CcmE"
-
Evidence questions CcmAB as a heme exporter.
"We also present evidence that questions the role of CcmAB as a heme exporter; yet, the transported substrate remains unknown."
Oxidase and periplasmic cytochrome assembly in Escherichia coli K-12: CydDC and CcmAB are not required for haem-membrane association.
-
ccmA deletion does not alter haem uptake kinetics into everted membrane vesicles, arguing against CcmAB-mediated haem export.
"suggesting that the activity of neither the CydDC nor CcmAB transporters is essential for haem export to the periplasm"
New insights into the role of CcmC, CcmD and CcmE in the haem delivery pathway during cytochrome c maturation by a complete mutational analysis of the conserved tryptophan-rich motif of CcmC.
-
The tryptophan-rich WGXXWXWD motif in the second periplasmic loop of CcmC is required for covalent haem incorporation into CcmE.
"Our results demonstrate the functional importance of the tryptophan-rich motif for haem transfer to CcmE."
Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation.
-
CcmC binds heme directly and co-immunoprecipitates with CcmE.
"Here, we report that the CcmC protein directly interacts with heme. We further show that CcmC co-immunoprecipitates with CcmE."
A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c.
CcmD is involved in complex formation between CcmC and the heme chaperone CcmE during cytochrome c maturation.
-
CcmC, CcmD and CcmE form a ternary complex.
"We demonstrate the formation of a ternary complex consisting of CcmCDE."
Global topology analysis of the Escherichia coli inner membrane proteome.
The membrane anchors of the heme chaperone CcmE and the periplasmic thioredoxin CcmG are functionally important.
ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis.
-
Without CcmA or CcmB, holo-CcmE is trapped on CcmC; CcmAB and ATP are needed for its release from a CcmA2B1C1 complex.
"In the absence of CcmA or CcmB, holo(haem)CcmE binds to CcmC in a stable dead-end complex, indicating high affinity binding of haem to CcmC."
Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE.
Topology and function of CcmD in cytochrome c maturation.
-
CcmD is a component of the CcmABCD complex and is required for holo-CcmE release, but not for CcmC-dependent heme transfer to CcmE.
"CcmD is not necessary for the CcmC-dependent transfer of heme to CcmE in the periplasm or for interaction of CcmE with CcmABC."
A conserved haem redox and trafficking pathway for cofactor attachment.
-
CcmC His60 and His184 are the axial ligands of heme in the purified CcmCDE complex, defining the CcmC external heme-binding domain.
"Haem in this holoCcmCDE complex is bound using periplasmic axial ligands His60 and His184 of CcmC, establishing that CcmC binds haem"
Probing heme delivery processes in cytochrome c biogenesis System I.
-
The CcmABC heme-transporter model is described as disproven.
"It was thought that CcmABC form a ATP-driven heme transporter,14 but this has since been disproven."
Structurally Mapping Endogenous Heme in the CcmCDE Membrane Complex for Cytochrome c Biogenesis.
Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation.
Biochemical mapping reveals a conserved heme transport mechanism via CcmCD in System I bacterial cytochrome c biogenesis.
Complexation of CcmB with CcmACD safeguards heme translocation for cytochrome c maturation.
-
CcmB overproduction drives heme efflux in S. oneidensis; E. coli CcmB homolog assays support heme handling in heterologous systems.
"Similar results were obtained from E. coli CcmB expressed from the same expression system"
Multiple phenotypic alterations caused by a c-type cytochrome maturation ccmC gene mutation in Pseudomonas aeruginosa.
-
A P. aeruginosa ccmC mutation eliminates detectable catalase production among several pleiotropic phenotypes.
"catalase production was undetectable, consistent with the increased sensitivity to hydrogen peroxide."