ID   CCMA_HAEDU              Reviewed;         210 AA.
AC   Q7VN12;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Cytochrome c biogenesis ATP-binding export protein CcmA {ECO:0000255|HAMAP-Rule:MF_01707};
DE            EC=7.6.2.5 {ECO:0000255|HAMAP-Rule:MF_01707};
DE   AltName: Full=Heme exporter protein A {ECO:0000255|HAMAP-Rule:MF_01707};
GN   Name=ccmA {ECO:0000255|HAMAP-Rule:MF_01707}; OrderedLocusNames=HD_0786;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the ABC transporter complex CcmAB involved in the
CC       biogenesis of c-type cytochromes; once thought to export heme, this
CC       seems not to be the case, but its exact role is uncertain. Responsible
CC       for energy coupling to the transport system. {ECO:0000255|HAMAP-
CC       Rule:MF_01707}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate;
CC         Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:456216; EC=7.6.2.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01707};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (CcmA) and
CC       two transmembrane proteins (CcmB). {ECO:0000255|HAMAP-Rule:MF_01707}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01707}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01707}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. CcmA exporter
CC       (TC 3.A.1.107) family. {ECO:0000255|HAMAP-Rule:MF_01707}.
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DR   EMBL; AE017143; AAP95689.1; -; Genomic_DNA.
DR   RefSeq; WP_010944739.1; NC_002940.2.
DR   AlphaFoldDB; Q7VN12; -.
DR   SMR; Q7VN12; -.
DR   STRING; 233412.HD_0786; -.
DR   EnsemblBacteria; AAP95689; AAP95689; HD_0786.
DR   KEGG; hdu:HD_0786; -.
DR   eggNOG; COG4133; Bacteria.
DR   HOGENOM; CLU_000604_1_2_6; -.
DR   OMA; GITHLPF; -.
DR   Proteomes; UP000001022; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015439; F:ABC-type heme transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR005895; ABC_transptr_haem_export_CcmA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43499; PTHR43499; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01189; ccmA; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51243; CCMA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane;
KW   Cytochrome c-type biogenesis; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..210
FT                   /note="Cytochrome c biogenesis ATP-binding export protein
FT                   CcmA"
FT                   /id="PRO_0000092181"
FT   DOMAIN          1..208
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
SQ   SEQUENCE   210 AA;  23847 MW;  22C8E50753D01D7B CRC64;
     MHLNQLVISH LACERGENRL FEGCHFSVSS GEWVQIEGHN GIGKTSLLRI LAGLALPVAG
     EVLWNNLSIH KQRDEYYAEL FYLGHYAGIK PELSAWENLR FYQKMQGLSL DDEALWFALD
     KVSLVERADL PCSYLSAGQQ RRVALAKLWL TQQKLWILDE PFTAIDNHGV GDLIMHIERH
     CSLGGMAIFT SHQTVESNKV RTLSLDQFKL