CCMA_PARDP
ID CCMA_PARDP Reviewed; 210 AA.
AC P52218; A1B1X0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=Pden_1413;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9043133; DOI=10.1099/00221287-143-2-563;
RA Page D., Pearce D.A., Norris H.A., Ferguson S.J.;
RT "The Paracoccus denitrificans ccmA, B and C genes: cloning and sequencing,
RT and analysis of the potential of their products to form a haem or apo-c-
RT type cytochrome transporter.";
RL Microbiology 143:563-576(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT.
RX PubMed=10589712; DOI=10.1099/00221287-145-11-3047;
RA Page M.D., Ferguson S.J.;
RT "Mutational analysis of the Paracoccus denitrificans c-type cytochrome
RT biosynthetic genes ccmABCDG: disruption of ccmC has distinct effects
RT suggesting a role for CcmC independent of CcmAB.";
RL Microbiology 145:3047-3057(1999).
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 ECO:0000269|PubMed:10589712}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z71971; CAA96502.1; -; Genomic_DNA.
DR EMBL; CP000489; ABL69514.1; -; Genomic_DNA.
DR RefSeq; WP_011747732.1; NC_008686.1.
DR AlphaFoldDB; P52218; -.
DR SMR; P52218; -.
DR STRING; 318586.Pden_1413; -.
DR PRIDE; P52218; -.
DR EnsemblBacteria; ABL69514; ABL69514; Pden_1413.
DR KEGG; pde:Pden_1413; -.
DR eggNOG; COG4133; Bacteria.
DR HOGENOM; CLU_000604_1_2_5; -.
DR OMA; NLAWLCA; -.
DR Proteomes; UP000000361; Chromosome 1.
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 1: Evidence at protein level;
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_0000092192"
FT DOMAIN 4..207
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
FT CONFLICT 34
FT /note="L -> V (in Ref. 1; CAA96502)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="L -> V (in Ref. 1; CAA96502)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="V -> GL (in Ref. 1; CAA96502)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..160
FT /note="ML -> IV (in Ref. 1; CAA96502)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..202
FT /note="RQSRP -> PAIAA (in Ref. 1; CAA96502)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 22169 MW; A2039284EB60FBE8 CRC64;
MNLLAVRDLA VARGGLRAVE GVCFNLNAGG ALVLRGPNGI GKTTLLRTLA GLQPLVSGVI
EAAPDAIAYA GHSDGLKPAL TVTENLRFWA EIFGGRNIDA ALEAMNLRDL ANRPAHALSA
GQKRRLGLAR LMVTGRPVWL LDEPTVSLDR DSVALFAAML RAHLGRGGAA VIATHIDLGL
PEAEILELGP FRASELRRQS RPAGFNEAFG
