CCMA_COLP3
ID CCMA_COLP3 Reviewed; 219 AA.
AC Q487I2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=CPS_1034;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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; CP000083; AAZ25480.1; -; Genomic_DNA.
DR RefSeq; WP_011041877.1; NC_003910.7.
DR AlphaFoldDB; Q487I2; -.
DR SMR; Q487I2; -.
DR STRING; 167879.CPS_1034; -.
DR EnsemblBacteria; AAZ25480; AAZ25480; CPS_1034.
DR KEGG; cps:CPS_1034; -.
DR HOGENOM; CLU_000604_1_2_6; -.
DR OMA; GITHLPF; -.
DR OrthoDB; 1833499at2; -.
DR Proteomes; UP000000547; 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..219
FT /note="Cytochrome c biogenesis ATP-binding export protein
FT CcmA"
FT /id="PRO_0000271920"
FT DOMAIN 10..218
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01707"
SQ SEQUENCE 219 AA; 24442 MW; 7B738CB802382F4A CRC64;
MSKKNSTPLI SAVNLTCIRE ERLLFDELSL QINAGDIVQV EGPNGSGKTS LLRILSGLSQ
PYDGQILYRE QLISHCREEF HQNLLYFGHL SGVKGEMTAE ENLDFNLALH GNKTQESLSY
LAKVNLSGFE ECLASHLSAG QHRRIALARL YQSNVPIWIL DEPFTAIDKQ GVASLERLFS
LHAERGGCVI LTTHQDLISI KPEQIKKITL DYSYDSAVD