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CYCM_BRADU
ID   CYCM_BRADU              Reviewed;         184 AA.
AC   P30323;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Cytochrome c homolog;
GN   Name=cycM; OrderedLocusNames=blr1423;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=USDA 110spc4;
RX   PubMed=1657867; DOI=10.1128/jb.173.21.6766-6772.1991;
RA   Bott M., Ritz D., Hennecke H.;
RT   "The Bradyrhizobium japonicum cycM gene encodes a membrane-anchored homolog
RT   of mitochondrial cytochrome c.";
RL   J. Bacteriol. 173:6766-6772(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: May be involved in electron transfer from bc1 complex to aa3.
CC       {ECO:0000269|PubMed:1657867}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1657867};
CC       Single-pass type II membrane protein {ECO:0000269|PubMed:1657867}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR   EMBL; M77189; AAA26198.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC46688.1; -; Genomic_DNA.
DR   PIR; A41331; A41331.
DR   RefSeq; NP_768063.1; NC_004463.1.
DR   RefSeq; WP_011084240.1; NZ_CP011360.1.
DR   AlphaFoldDB; P30323; -.
DR   SMR; P30323; -.
DR   STRING; 224911.27349675; -.
DR   EnsemblBacteria; BAC46688; BAC46688; BAC46688.
DR   GeneID; 64021299; -.
DR   KEGG; bja:blr1423; -.
DR   PATRIC; fig|224911.44.peg.851; -.
DR   eggNOG; COG3474; Bacteria.
DR   HOGENOM; CLU_060944_4_0_5; -.
DR   InParanoid; P30323; -.
DR   OMA; KGYIPGT; -.
DR   PhylomeDB; P30323; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..184
FT                   /note="Cytochrome c homolog"
FT                   /id="PRO_0000108415"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..184
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         84
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         87
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         88
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         151
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   184 AA;  19098 MW;  2ECDCFA564389824 CRC64;
     MDSFELNKIL GAVLGTCLIL LVTSFTANAL FSPKMPEKPG FEIAVKEDAG HGKEGGAAAA
     ASEPIEKLLQ TASVEKGAAA AKKCGACHTF EKGGPNRVGP NLYGVVGEAR GEGRNGFNFS
     AAMKGKGGTW TFDDLNKFIA NPKGFIPGTA MGFAGIPKDS ERADVIAYLN SLSEHPKPLP
     TASK
 
 
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