CCMA_PSEPG
ID CCMA_PSEPG Reviewed; 210 AA.
AC P95487; B0KQ31;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 117.
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};
GN OrderedLocusNames=PputGB1_3896;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-210.
RX PubMed=9758767; DOI=10.1128/aem.64.10.3556-3562.1998;
RA de Vrind J.P.M., Brouwers G.J., Corstjens P.L.A.M., den Dulk J.,
RA de Vrind-de Jong E.W.;
RT "The cytochrome c maturation operon is involved in manganese oxidation in
RT Pseudomonas putida GB-1.";
RL Appl. Environ. Microbiol. 64:3556-3562(1998).
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 ---------------------------------------------------------------------------
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; CP000926; ABY99786.1; -; Genomic_DNA.
DR EMBL; U85716; AAC63581.1; -; Genomic_DNA.
DR RefSeq; WP_012273478.1; NC_010322.1.
DR AlphaFoldDB; P95487; -.
DR SMR; P95487; -.
DR STRING; 76869.PputGB1_3896; -.
DR EnsemblBacteria; ABY99786; ABY99786; PputGB1_3896.
DR GeneID; 66677087; -.
DR KEGG; ppg:PputGB1_3896; -.
DR eggNOG; COG4133; Bacteria.
DR HOGENOM; CLU_000604_1_2_6; -.
DR OMA; NLAWLCA; -.
DR Proteomes; UP000002157; 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; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
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; 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..210
FT /note="Cytochrome c biogenesis ATP-binding export protein
FT CcmA"
FT /id="PRO_0000092197"
FT DOMAIN 3..205
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
FT CONFLICT 60..69
FT /note="QILLGGKPLA -> ADPAGAQRLR (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> R (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="A -> P (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="H -> D (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..115
FT /note="AIWA -> RL (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..132
FT /note="CHT -> VPY (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..151
FT /note="CP -> AR (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..174
FT /note="VAQLEAH -> AGAAGSS (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="T -> H (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> P (in Ref. 2; AAC63581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 22746 MW; F2FA7F68827F0DCB CRC64;
MTLHLQAAGL ACERDWRLLF EQLDFELGAG DMLQISGPNG SGKTSLLRLL AGLMQPTAGQ
ILLGGKPLAE QRHALASILL WIGHAAGIKD LLTAEENLTW LCALHQPASR EAIWAALEAV
GLRGFEDVPC HTLSAGQQRR VALARLHLAC PPLWILDEPF TALDKQGVAQ LEAHLAAHCE
QGGTVVLTTH HTLERKPSGY RELNLGQWAA
