CGR1_EGGLE
ID CGR1_EGGLE Reviewed; 216 AA.
AC C8WLM0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Cytochrome c-type protein Cgr1 {ECO:0000305};
DE AltName: Full=Cardiac glycoside reductase operon protein 1 {ECO:0000303|PubMed:23869020};
GN Name=cgr1 {ECO:0000303|PubMed:23869020};
GN OrderedLocusNames=Elen_2528 {ECO:0000312|EMBL:ACV56483.1};
OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=479437;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC
RC 11813 / VPI 0255 / 1899 B;
RX PubMed=21304654; DOI=10.4056/sigs.33592;
RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT 0255).";
RL Stand. Genomic Sci. 1:174-182(2009).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC
RC 11813 / VPI 0255 / 1899 B;
RX PubMed=23869020; DOI=10.1126/science.1235872;
RA Haiser H.J., Gootenberg D.B., Chatman K., Sirasani G., Balskus E.P.,
RA Turnbaugh P.J.;
RT "Predicting and manipulating cardiac drug inactivation by the human gut
RT bacterium Eggerthella lenta.";
RL Science 341:295-298(2013).
RN [3]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC
RC 11813 / VPI 0255 / 1899 B;
RX PubMed=29761785; DOI=10.7554/elife.33953;
RA Koppel N., Bisanz J.E., Pandelia M.E., Turnbaugh P.J., Balskus E.P.;
RT "Discovery and characterization of a prevalent human gut bacterial enzyme
RT sufficient for the inactivation of a family of plant toxins.";
RL Elife 7:E33953-E33953(2018).
CC -!- FUNCTION: Probably transfers electrons from a membrane-associated
CC electron donor (e.g. the membrane quinone pool) to the [4Fe-4S] cluster
CC of the Cgr2 reductase via its covalently bound heme groups.
CC {ECO:0000305|PubMed:29761785}.
CC -!- SUBUNIT: May form a membrane-associated complex with Cgr2.
CC {ECO:0000305|PubMed:29761785}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Is highly up-regulated by digoxin and other cardiac
CC glycosides containing unsaturated butyrolactone rings, such as
CC digitoxin, digoxigenin, and, to a lesser extent, ouabain. Is repressed
CC by arginine but not by ornithine. Part of an operon that consists of
CC cgr1 and cgr2. {ECO:0000269|PubMed:23869020}.
CC -!- PTM: Binds 5 heme groups per subunit. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the multiheme cytochrome c family.
CC {ECO:0000305}.
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DR EMBL; CP001726; ACV56483.1; -; Genomic_DNA.
DR RefSeq; WP_015761236.1; NC_013204.1.
DR AlphaFoldDB; C8WLM0; -.
DR STRING; 479437.Elen_2528; -.
DR EnsemblBacteria; ACV56483; ACV56483; Elen_2528.
DR KEGG; ele:Elen_2528; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_107073_0_0_11; -.
DR OMA; HEDIRMD; -.
DR OrthoDB; 1683334at2; -.
DR BioCyc; ELEN479437:G1GFY-2551-MON; -.
DR Proteomes; UP000001377; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR012286; Tetrahaem_cytochrome.
DR Pfam; PF14537; Cytochrom_c3_2; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..216
FT /note="Cytochrome c-type protein Cgr1"
FT /id="PRO_0000449513"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 46
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 50
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 51
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 95
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 98
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 99
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 142
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 147
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 148
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 176
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 179
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 180
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 190
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 193
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 194
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 23840 MW; 90B6CE612CA4FC90 CRC64;
MAEEPVVIGD PAPRTRKWPI VVGVVVVVLI AAGAGFWVWH EQPSFCAAIC HTPMDEYLET
YEQEAGTAGV DKWGNEVANT NAMLAVSHKA QGKDCMACHV PTLSEQMSEG MNWVTGNYVY
PLEERDTEML TEARGVDADE FCLNESCHNL TRDDLIKATS DMEFNPHQPQ HGEIECSECH
KAHRASVMYC TQCHSEAEVP EGWLTVAEAN KLSTAA
