GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

file:ECOLI/ccmE/ccmE-uniprot.txt

UniProtKB entry P69490 (CcmE, Escherichia coli K-12)

Curated function, subunit (CcmCD ternary complex, CcmF interaction) and HAMAP family classification of CcmE.

PMID:11744735

A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c.

CcmF co-immunoprecipitates with CcmE and CcmH, placing holo-CcmE at the CcmFH heme-lyase complex.

PMID:15513913

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 during heme delivery to CcmE.

PMID:16364305

The membrane anchors of the heme chaperone CcmE and the periplasmic thioredoxin CcmG are functionally important.

CcmE is a monotopic membrane protein whose anchor is needed for efficient heme receipt but not for heme delivery to cytochrome c.

PMID:16824107

ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis.

CcmAB-dependent ATP hydrolysis releases holo-CcmE from CcmC; without CcmA or CcmB holo-CcmE is trapped in a dead-end complex.

PMID:19629033

A conserved haem redox and trafficking pathway for cofactor attachment.

Purified CcmCDE complexes show CcmC His60/His184 as heme axial ligands and CcmE His130 as the covalent adduct; holo-CcmE heme is oxidized.

PMID:24044352

Probing heme delivery processes in cytochrome c biogenesis System I.

Reviews the CcmABCDE heme-delivery model and states that the CcmABC heme-transporter model has been disproven.

PMID:9712585

Prototype of a heme chaperone essential for cytochrome c maturation.

CcmE binds heme covalently via a histidine in the periplasm and delivers it to apocytochrome c.

PMID:10339610

Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB.

PMID:37626034

Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation.

E. coli CcmABCD/E structures support ATP-coupled conformational changes and propose a heme floppase mechanism.

"suggest that this unusual ABC transporter acts as a heme floppase"

PMID:40167305

Biochemical mapping reveals a conserved heme transport mechanism via CcmCD in System I bacterial cytochrome c biogenesis.

The E. coli biochemical mapping results do not support CcmB as the heme-acceptance component of System I; this is evidence against that model, not an MR-1 transport assay.

"do not support a role for CcmB in heme acceptance for System I"