CCME_BRUAB
ID CCME_BRUAB Reviewed; 165 AA.
AC Q57ED2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=BruAb1_0627;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(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; AE017223; AAX74002.1; -; Genomic_DNA.
DR RefSeq; WP_002963757.1; NC_006932.1.
DR AlphaFoldDB; Q57ED2; -.
DR SMR; Q57ED2; -.
DR EnsemblBacteria; AAX74002; AAX74002; BruAb1_0627.
DR GeneID; 45124066; -.
DR KEGG; bmb:BruAb1_0627; -.
DR HOGENOM; CLU_079503_1_1_5; -.
DR OMA; HVEFAVH; -.
DR Proteomes; UP000000540; Chromosome I.
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..165
FT /note="Cytochrome c-type biogenesis protein CcmE"
FT /id="PRO_0000238798"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT TRANSMEM 30..50
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT TOPO_DOM 51..165
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT BINDING 143
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT BINDING 147
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 165 AA; 17977 MW; F67EB3C3641DCC6F CRC64;
MSATAEQNAR NPKGKGGFAR TVSQRKRKRL FLIGGALAVL AVAVGLMLTA FNQDIRFFRT
PADLTEQDMT SGARFRLGGL VEEGSVSRTG SELRFTVTDT IKTVKVVFEG IPPDLFREGQ
GVVAEGRFGS DGLFRADNVL AKHDENYVPK DLADSLKKKG VWEGK
