CCMA_ZYMMO
ID CCMA_ZYMMO Reviewed; 221 AA.
AC Q5NQX0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 114.
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}; Synonyms=cycV;
GN OrderedLocusNames=ZMO0260;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; AE008692; AAV88884.2; -; Genomic_DNA.
DR RefSeq; WP_011240202.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NQX0; -.
DR STRING; 264203.ZMO0260; -.
DR EnsemblBacteria; AAV88884; AAV88884; ZMO0260.
DR GeneID; 58026130; -.
DR KEGG; zmo:ZMO0260; -.
DR eggNOG; COG4133; Bacteria.
DR HOGENOM; CLU_000604_1_2_5; -.
DR OMA; GITHLPF; -.
DR OrthoDB; 1833499at2; -.
DR Proteomes; UP000001173; 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;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..221
FT /note="Cytochrome c biogenesis ATP-binding export protein
FT CcmA"
FT /id="PRO_0000092228"
FT DOMAIN 14..221
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
SQ SEQUENCE 221 AA; 23936 MW; 16040324E3584974 CRC64;
MGRKRLSDFG NARLACHDVS CLRGDRLLFT HLSFEVKAGE AVLITGANGI GKSSLLRLLA
GFLKPFSGHI EKWGRVAFAD EALAMDRHLP LEKALAYWAA LDGVLGAEKE AMAVMALDIL
ADSPVRLLST GQRKRAVLAR LLASQAAIWL LDEPANGLDA ASVRALIEMI EHHRQKGGII
LAVSHQGLDM ADYKTLSLEN FVANSGQSSG FFDLLDESHF S