ID   CCME_ROSDO              Reviewed;         147 AA.
AC   Q163W5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=RD1_3226;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01959}; Single-pass type II membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01959}; Periplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_01959}.
CC   -!- SIMILARITY: Belongs to the CcmE/CycJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01959}.
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DR   EMBL; CP000362; ABG32728.1; -; Genomic_DNA.
DR   RefSeq; WP_011569344.1; NZ_FOOO01000004.1.
DR   AlphaFoldDB; Q163W5; -.
DR   SMR; Q163W5; -.
DR   STRING; 375451.RD1_3226; -.
DR   EnsemblBacteria; ABG32728; ABG32728; RD1_3226.
DR   KEGG; rde:RD1_3226; -.
DR   eggNOG; COG2332; Bacteria.
DR   HOGENOM; CLU_079503_1_1_5; -.
DR   OMA; HVEFAVH; -.
DR   OrthoDB; 1724595at2; -.
DR   Proteomes; UP000007029; 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 inner membrane; Cell membrane; Cytochrome c-type biogenesis; Heme;
KW   Iron; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..147
FT                   /note="Cytochrome c-type biogenesis protein CcmE"
FT                   /id="PRO_1000070847"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   TRANSMEM        10..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   TOPO_DOM        31..147
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   BINDING         123
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   BINDING         127
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   147 AA;  15907 MW;  7AA894E199BFA4AC CRC64;
     MKNLKKQRRI QVIALATVAL VLSTALIGYA MRDGINFFRA PTQILAEPPA PTEVFRIGGL
     VEEGSIVRGQ GETIRFSVTD GNGVVPVTYT GVLPDLFEEN QGMVGTGSYI NGVFEASEIL
     AKHDETYMPA EVVDMLKEQG VYKGTEG