CCMA_RHOPB
ID CCMA_RHOPB Reviewed; 200 AA.
AC Q21CV6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
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=RPC_0205;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD85780.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000301; ABD85780.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041802278.1; NC_007925.1.
DR AlphaFoldDB; Q21CV6; -.
DR SMR; Q21CV6; -.
DR STRING; 316056.RPC_0205; -.
DR EnsemblBacteria; ABD85780; ABD85780; RPC_0205.
DR KEGG; rpc:RPC_0205; -.
DR eggNOG; COG4133; Bacteria.
DR HOGENOM; CLU_000604_1_2_5; -.
DR OMA; NLAWLCA; -.
DR OrthoDB; 1833499at2; -.
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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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; Translocase;
KW Transport.
FT CHAIN 1..200
FT /note="Cytochrome c biogenesis ATP-binding export protein
FT CcmA"
FT /id="PRO_0000271949"
FT DOMAIN 1..199
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
SQ SEQUENCE 200 AA; 20551 MW; 8485457DD4439AFF CRC64;
MRLTGRGLRC VRGGRQVFAG LDVDAAAGEA VAVVGANGAG KTSLLRLIAG LLALAGGAIA
LEGGDSELTL AEQAHYLGHR DALKPSLSVA ENLIFWQQFL GGEPADAQAS LAAVGLGHIA
HLPAAYLSAG QRRRLSLARL TAVRRPLWLL DEPTSALDAE GQAMFARLMT AHLESGGLLV
AATHTPLGIA ARELRIGGAA