CCMAE_SALCH
ID CCMAE_SALCH Reviewed; 336 AA.
AC Q57I19;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative bifunctional cytochrome c-type biogenesis protein CcmAE;
DE Includes:
DE RecName: Full=Cytochrome c biogenesis ATP-binding export protein CcmA 2;
DE EC=7.6.2.5 {ECO:0000305};
DE AltName: Full=Heme exporter protein A 2;
DE Includes:
DE RecName: Full=Cytochrome c-type biogenesis protein CcmE 2;
DE AltName: Full=Cytochrome c maturation protein E 2;
DE AltName: Full=Heme chaperone CcmE 2;
GN Name=ccmAE; Synonyms=ccmA2, ccmE2; OrderedLocusNames=SCH_3737;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(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 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Heme chaperone required for the biogenesis of c-type
CC cytochromes. Transiently binds heme delivered by CcmC and transfers the
CC heme to apo-cytochromes in a process facilitated by CcmF and CcmH (By
CC similarity). {ECO:0000250}.
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:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ABC transporter
CC superfamily. CcmA exporter (TC 3.A.1.107) family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the CcmE/CycJ family.
CC {ECO:0000305}.
CC -!- CAUTION: This sequence is a fusion of the duplicated copies ccmA2 and
CC ccmE2, however, important parts of the proteins are missing and it is
CC therefore probably not functional. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX67643.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017220; AAX67643.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_024131381.1; NC_006905.1.
DR AlphaFoldDB; Q57I19; -.
DR SMR; Q57I19; -.
DR EnsemblBacteria; AAX67643; AAX67643; SCH_3737.
DR KEGG; sec:SCH_3737; -.
DR HOGENOM; CLU_071298_0_0_6; -.
DR Proteomes; UP000000538; 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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR GO; GO:0017003; P:protein-heme linkage; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01959; CcmE; 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; IPR004329; CcmE.
DR InterPro; IPR036127; CcmE-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43499; PTHR43499; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03100; CcmE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82093; SSF82093; 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 5: Uncertain;
KW ATP-binding; Cell inner membrane; Cell membrane;
KW Cytochrome c-type biogenesis; Heme; Iron; Membrane; Metal-binding;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..336
FT /note="Putative bifunctional cytochrome c-type biogenesis
FT protein CcmAE"
FT /id="PRO_0000238860"
FT DOMAIN 2..242
FT /note="ABC transporter"
FT REGION 1..199
FT /note="Cytochrome c biogenesis ATP-binding export protein
FT CcmA 2"
FT REGION 196..336
FT /note="Cytochrome c-type biogenesis protein CcmE 2"
FT REGION 307..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 307
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 37197 MW; 26E359D6F50FB952 CRC64;
MLEARDLYCE RDERTLFRGL SFTVDAGEWV QVTGGNGAGK TTLLRLLTGL ARPDGGEVYW
QGEPLRRVRD SFHRSLLWIG HQPGIKTRLT ARENLHFFHP GDGARLPEAL AQAGLAGFED
VPVARLSAGQ QRRVALARLW LTRAALWVLD EPFTAIDVNG VARLTRRMAA HTAQGGMVIL
TTHQPLPGAA DTVRRLALTT ALVLYALRAN IDLFYTPGEI LYGKRETQQL PAVGQRLRVG
GMVMPGSVRR DPDSLKVNFS LYDAEGSVTV SYEGILPDLF REGQGVVVQG TLEKGNHVLA
HEVLAKHDEN YTPPEVEKAM QENHRRPQRV DKDTSS
