ID   CCME_RHOCB              Reviewed;         150 AA.
AC   Q9LA01; D5ANG5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=RCAP_rcc00554;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF HIS-123.
RC   STRAIN=MT1131;
RX   PubMed=10632883; DOI=10.1046/j.1365-2958.2000.01683.x;
RA   Deshmukh M., Brasseur G., Daldal F.;
RT   "Novel Rhodobacter capsulatus genes required for the biogenesis of various
RT   c-type cytochromes.";
RL   Mol. Microbiol. 35:123-138(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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, ECO:0000269|PubMed:10632883}.
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; AF156104; AAF26221.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE84319.1; -; Genomic_DNA.
DR   RefSeq; WP_013066298.1; NC_014034.1.
DR   AlphaFoldDB; Q9LA01; -.
DR   SMR; Q9LA01; -.
DR   STRING; 272942.RCAP_rcc00554; -.
DR   EnsemblBacteria; ADE84319; ADE84319; RCAP_rcc00554.
DR   GeneID; 31489505; -.
DR   KEGG; rcp:RCAP_rcc00554; -.
DR   eggNOG; COG2332; Bacteria.
DR   HOGENOM; CLU_079503_1_1_5; -.
DR   OMA; TFRVGGM; -.
DR   OrthoDB; 1724595at2; -.
DR   Proteomes; UP000002361; 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   1: Evidence at protein level;
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..150
FT                   /note="Cytochrome c-type biogenesis protein CcmE"
FT                   /id="PRO_0000238851"
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..150
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"
FT   MUTAGEN         123
FT                   /note="H->A: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:10632883"
SQ   SEQUENCE   150 AA;  15978 MW;  57E4E3724E79B934 CRC64;
     MRNLKKTRRI QILLVAGGAL VLSTALIGYG MRDGINFFRA PSQIVAEPPA AGEVFRLGGL
     VEAGTLVRGQ GEEITFKVTD GGASVPVTFT GVLPDLFGEG KGMVGTGEMV EGTFVAREIL
     AKHDENYMPK EVTEALKEQG VYRDPAQPEG