ID   CCME1_SALCH             Reviewed;         159 AA.
AC   Q57MA1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Cytochrome c-type biogenesis protein CcmE 1 {ECO:0000255|HAMAP-Rule:MF_01959};
DE   AltName: Full=Cytochrome c maturation protein E 1 {ECO:0000255|HAMAP-Rule:MF_01959};
DE   AltName: Full=Heme chaperone CcmE 1 {ECO:0000255|HAMAP-Rule:MF_01959};
GN   Name=ccmE1 {ECO:0000255|HAMAP-Rule:MF_01959};
GN   Synonyms=cycJ1 {ECO:0000255|HAMAP-Rule:MF_01959};
GN   OrderedLocusNames=SCH_2255;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX66161.1; -; Genomic_DNA.
DR   RefSeq; WP_001053608.1; NC_006905.1.
DR   AlphaFoldDB; Q57MA1; -.
DR   SMR; Q57MA1; -.
DR   EnsemblBacteria; AAX66161; AAX66161; SCH_2255.
DR   KEGG; sec:SCH_2255; -.
DR   HOGENOM; CLU_079503_1_0_6; -.
DR   OMA; HVEFAVH; -.
DR   Proteomes; UP000000538; 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; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..159
FT                   /note="Cytochrome c-type biogenesis protein CcmE 1"
FT                   /id="PRO_0000238859"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   TOPO_DOM        30..159
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   REGION          130..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   BINDING         134
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   159 AA;  17758 MW;  F5A1D5422876DFED CRC64;
     MNLRRKNRLW VVCAVLAGLA LTTALVLYAL RANIDLFYTP GEILYGKRET QQLPAVGQRL
     RVGGMVMPGS VRRDPDSLKV NFSLYDAEGS VTVSYEGILP DLFREGQGVV VQGTLEKGNH
     VLAHEVLAKH DENYTPPEVE KAMQENHRRP QRVDKDTSS