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CCME2_XANAC
ID   CCME2_XANAC             Reviewed;         156 AA.
AC   Q8PK49;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cytochrome c-type biogenesis protein CcmE 2 {ECO:0000255|HAMAP-Rule:MF_01959};
DE   AltName: Full=Cytochrome c maturation protein E 2 {ECO:0000255|HAMAP-Rule:MF_01959};
DE   AltName: Full=Heme chaperone CcmE 2 {ECO:0000255|HAMAP-Rule:MF_01959};
GN   Name=ccmE2 {ECO:0000255|HAMAP-Rule:MF_01959};
GN   Synonyms=cycJ2 {ECO:0000255|HAMAP-Rule:MF_01959};
GN   OrderedLocusNames=XAC2327;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01959}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01959}; Single-pass type II membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01959}; Periplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_01959}.
CC   -!- SIMILARITY: Belongs to the CcmE/CycJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01959}.
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DR   EMBL; AE008923; AAM37180.1; -; Genomic_DNA.
DR   RefSeq; WP_011051512.1; NC_003919.1.
DR   AlphaFoldDB; Q8PK49; -.
DR   SMR; Q8PK49; -.
DR   STRING; 190486.XAC2327; -.
DR   EnsemblBacteria; AAM37180; AAM37180; XAC2327.
DR   GeneID; 66911446; -.
DR   KEGG; xac:XAC2327; -.
DR   eggNOG; COG2332; Bacteria.
DR   HOGENOM; CLU_079503_1_1_6; -.
DR   OMA; VTIHFRV; -.
DR   Proteomes; UP000000576; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   HAMAP; MF_01959; CcmE; 1.
DR   InterPro; IPR004329; CcmE.
DR   InterPro; IPR036127; CcmE-like_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR34128; PTHR34128; 1.
DR   Pfam; PF03100; CcmE; 1.
DR   SUPFAM; SSF82093; SSF82093; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis; Heme;
KW   Iron; Membrane; Metal-binding; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..156
FT                   /note="Cytochrome c-type biogenesis protein CcmE 2"
FT                   /id="PRO_0000238880"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   TOPO_DOM        30..156
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   REGION          136..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         123
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01959"
FT   BINDING         127
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:0000255|HAMAP-Rule:MF_01959"
SQ   SEQUENCE   156 AA;  17090 MW;  2641E2585E3A0E44 CRC64;
     MNPQRRRRLW LVLALVLAGG LATTLVAMAL QRNVAYLYTP SEVLRGDAGA HSRFRLGGMV
     EKGSFKRASG SLEAQFRVTD GDAQLSVSYD RILPDLFREG QAVVATGRMQ HGIFVAEDVL
     AKHDETYMPK EVADKMGSAH RKHDVPAAAG QVGERQ
 
 
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