ID   CCME_ACTP2              Reviewed;         181 AA.
AC   A3N216;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=APL_1368;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN74452.1; -; Genomic_DNA.
DR   RefSeq; WP_009874921.1; NC_009053.1.
DR   AlphaFoldDB; A3N216; -.
DR   SMR; A3N216; -.
DR   STRING; 416269.APL_1368; -.
DR   EnsemblBacteria; ABN74452; ABN74452; APL_1368.
DR   KEGG; apl:APL_1368; -.
DR   PATRIC; fig|416269.6.peg.1426; -.
DR   eggNOG; COG2332; Bacteria.
DR   HOGENOM; CLU_079503_1_0_6; -.
DR   OMA; HVEFAVH; -.
DR   Proteomes; UP000001432; 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..181
FT                   /note="Cytochrome c-type biogenesis protein CcmE"
FT                   /id="PRO_1000070800"
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..181
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   REGION          135..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         131
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   BINDING         135
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   181 AA;  19786 MW;  7D44582EEA324767 CRC64;
     MNPRRKSRLK VVVSIIFGVA VAAGLMLYAL SQNIDLFYTP SEIVNGKNDD PDQKPEVGQR
     IRVGGMVVEG SVKRDDKTLK VEFEANDIGP SITVEYEGIL PDLFREGQGI VAQGVLIEPT
     RLKATEVLAK HDENYMPPEL GDKLKEQHGA AGISEADLKG TSARDKAEIE RTLKTLQGEA
     N