ID S5S7K9_RHIET Unreviewed; 431 AA.
AC S5S7K9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Cytochrome-c domain-containing protein {ECO:0000313|EMBL:AGS25920.1};
GN ORFNames=REMIM1_PF00252 {ECO:0000313|EMBL:AGS25920.1};
OS Rhizobium etli bv. mimosae str. Mim1.
OG Plasmid pRetMIM1f {ECO:0000313|EMBL:AGS25920.1,
OG ECO:0000313|Proteomes:UP000015261}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=1328306 {ECO:0000313|EMBL:AGS25920.1, ECO:0000313|Proteomes:UP000015261};
RN [1] {ECO:0000313|EMBL:AGS25920.1, ECO:0000313|Proteomes:UP000015261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mim1 {ECO:0000313|EMBL:AGS25920.1,
RC ECO:0000313|Proteomes:UP000015261};
RC PLASMID=Plasmid pRetMIM1f {ECO:0000313|Proteomes:UP000015261};
RA Rogel M.A., Bustos P., Santamaria R.I., Gonzalez V., Romero D.,
RA Cevallos M.A., Lozano L., Ormeno-Orrillo E., Martinez-Romero E.;
RT "Genomic basis of Rhizobium etli symbiovar mimosae and its prevalence among
RT Phaseolus vulgaris nodule bacteria.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR000018-50};
CC Note=Binds 3 heme c groups covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000018-50};
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DR EMBL; CP005956; AGS25920.1; -; Genomic_DNA.
DR RefSeq; WP_020919291.1; NC_021911.1.
DR AlphaFoldDB; S5S7K9; -.
DR KEGG; rel:REMIM1_PF00252; -.
DR PATRIC; fig|1328306.3.peg.6345; -.
DR HOGENOM; CLU_028594_0_0_5; -.
DR Proteomes; UP000015261; Plasmid pRetMIM1f.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR PANTHER; PTHR35008:SF8; BLL4482 PROTEIN; 1.
DR PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR Pfam; PF00034; Cytochrom_C; 2.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR SUPFAM; SSF46626; Cytochrome c; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000018-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000018-51};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000018-51}; Plasmid {ECO:0000313|EMBL:AGS25920.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..149
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 191..300
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 326..413
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 304..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 63
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 64
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
FT BINDING 206
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 209
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 210
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
FT BINDING 339
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 342
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 343
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
SQ SEQUENCE 431 AA; 46350 MW; 1E9D04DD5DE2D09B CRC64;
MTIRNNFSFV AAAAIVLCLI GAGLFFFIPH RLDQVVATAK QPVGDALIAR GEYLATAADC
AACHTTKGGK PFAGGLAFKL PFGTIYSSNI TPDSQHGIGG WSESEFVRAV KSGVGKHGED
LYPAFPYTSY ALLSDDDVLA IFAYLKTLAP AASQAQQSDL AFPFDQRWLM RGWKLLFMPR
NEHRRDPTRS EEWNRGAYLA EALAHCGECH TPRGLMFERK QSQALSGGIV EGWRAWNITS
DRENGVGAWS DEELASYLST GHAQGRGSAS GGMREAVDLS LSKLPSDDIR AMITYLRTVP
PVAGEPELRK SSNPKEKPVR LQSSDAGVDL GRRIFAGACA SCHGWEAKGQ ANPRAAIAGA
HAFSDPDAAN IIRVVLEGSS DGSNTPGSTM PAFKAMYSDE EVAALANFMV SRFGGKQPTA
TADDVRTARQ R
//
