ID   CCME_DEIDV              Reviewed;         158 AA.
AC   C1D1H5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Cytochrome c-type biogenesis protein CcmE {ECO:0000255|HAMAP-Rule:MF_01959};
DE   AltName: Full=Cytochrome c maturation protein E {ECO:0000255|HAMAP-Rule:MF_01959};
DE   AltName: Full=Heme chaperone CcmE {ECO:0000255|HAMAP-Rule:MF_01959};
GN   Name=ccmE {ECO:0000255|HAMAP-Rule:MF_01959};
GN   Synonyms=cycJ {ECO:0000255|HAMAP-Rule:MF_01959};
GN   OrderedLocusNames=Deide_08310;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- FUNCTION: Heme chaperone required for the biogenesis of c-type
CC       cytochromes. Transiently binds heme delivered by CcmC and transfers the
CC       heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
CC       {ECO:0000255|HAMAP-Rule:MF_01959}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01959};
CC       Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_01959}.
CC   -!- SIMILARITY: Belongs to the CcmE/CycJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01959}.
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DR   EMBL; CP001114; ACO45699.1; -; Genomic_DNA.
DR   RefSeq; WP_012692822.1; NC_012526.1.
DR   AlphaFoldDB; C1D1H5; -.
DR   SMR; C1D1H5; -.
DR   STRING; 546414.Deide_08310; -.
DR   PaxDb; C1D1H5; -.
DR   EnsemblBacteria; ACO45699; ACO45699; Deide_08310.
DR   KEGG; ddr:Deide_08310; -.
DR   eggNOG; COG2332; Bacteria.
DR   HOGENOM; CLU_079503_2_0_0; -.
DR   OMA; HVEFAVH; -.
DR   OrthoDB; 1724595at2; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   GO; GO:0017003; P:protein-heme linkage; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_01959; CcmE; 1.
DR   InterPro; IPR004329; CcmE.
DR   InterPro; IPR036127; CcmE-like_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR34128; PTHR34128; 1.
DR   Pfam; PF03100; CcmE; 1.
DR   SUPFAM; SSF82093; SSF82093; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cytochrome c-type biogenesis; Heme; Iron; Membrane;
KW   Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..158
FT                   /note="Cytochrome c-type biogenesis protein CcmE"
FT                   /id="PRO_1000216212"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   TRANSMEM        24..44
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   TOPO_DOM        45..158
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         137
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   BINDING         141
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
SQ   SEQUENCE   158 AA;  17440 MW;  7DEF153151E793CD CRC64;
     MTRPDSGSSP APLSEARRRK RNPLPTVLGI TALLGLAGFI AFGNLNKSLE YFVTPTEYQQ
     QAAQLKGRPV RIGGLVKAVK YNPQSLELSF TVTDGGASFP VRYRGAVSDL FKENQGVVVR
     GEFEGQTFQA RELIVKHSEQ YDVPKTQAEL RDLLEQSE