CCME_SHEON
ID CCME_SHEON Reviewed; 161 AA.
AC Q8EK44; O52690;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cytochrome c-type biogenesis protein CcmE;
DE AltName: Full=Cytochrome c maturation protein E;
DE AltName: Full=Heme chaperone CcmE;
GN Name=ccmE; Synonyms=cycJ; OrderedLocusNames=SO_0259;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MR-1;
RA Saffarini D.A., McCool J., Tsongalis J.;
RT "Cytochrome c maturation in the metal reducer Shewanella putrefaciens.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [3]
RP STRUCTURE BY NMR OF 30-161.
RX PubMed=12427019; DOI=10.1021/bi026362w;
RA Arnesano F., Banci L., Barker P.D., Bertini I., Rosato A., Su X.C.,
RA Viezzoli M.S.;
RT "Solution structure and characterization of the heme chaperone CcmE.";
RL Biochemistry 41:13587-13594(2002).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC type II membrane protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CcmE/CycJ family. {ECO:0000305}.
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DR EMBL; AF044582; AAC02697.1; -; Genomic_DNA.
DR EMBL; AE014299; AAN53344.1; -; Genomic_DNA.
DR RefSeq; NP_715899.1; NC_004347.2.
DR RefSeq; WP_011070633.1; NZ_CP053946.1.
DR PDB; 1J6Q; NMR; -; A=30-161.
DR PDB; 1LM0; NMR; -; A=30-161.
DR PDBsum; 1J6Q; -.
DR PDBsum; 1LM0; -.
DR AlphaFoldDB; Q8EK44; -.
DR BMRB; Q8EK44; -.
DR SMR; Q8EK44; -.
DR STRING; 211586.SO_0259; -.
DR PaxDb; Q8EK44; -.
DR KEGG; son:SO_0259; -.
DR PATRIC; fig|211586.12.peg.250; -.
DR eggNOG; COG2332; Bacteria.
DR HOGENOM; CLU_079503_1_0_6; -.
DR OMA; HVEFAVH; -.
DR OrthoDB; 1724595at2; -.
DR PhylomeDB; Q8EK44; -.
DR BioCyc; SONE211586:G1GMP-248-MON; -.
DR EvolutionaryTrace; Q8EK44; -.
DR Proteomes; UP000008186; 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 3D-structure; Cell inner membrane; Cell membrane;
KW Cytochrome c-type biogenesis; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..161
FT /note="Cytochrome c-type biogenesis protein CcmE"
FT /id="PRO_0000238864"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..161
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 138..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..154
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:0000250"
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:0000250"
FT TURN 40..46
FT /evidence="ECO:0007829|PDB:1J6Q"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:1J6Q"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1J6Q"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1J6Q"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1J6Q"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1J6Q"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1LM0"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:1J6Q"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1J6Q"
SQ SEQUENCE 161 AA; 17358 MW; 9B7FB4604F2A0629 CRC64;
MNPRRKKRLT LAVALIGGVA AIASLLLYAL NSNLNLFYTP SEIVNGKTDT GVKPEAGQRI
RVGGMVTVGS MVRDPNSLHV QFAVHDSLGG EILVTYDDLL PDLFREGQGI VAQGVLGEDG
KLAATEVLAK HDENYMPPEV AEAMGQKHEK LDYSQQKSAT Q
