ID I4WCL5_9GAMM Unreviewed; 238 AA.
AC I4WCL5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Ubiquinol-cytochrome c reductase, cytochrome c1 subunit {ECO:0000313|EMBL:EIL97206.1};
GN ORFNames=UU5_05618 {ECO:0000313|EMBL:EIL97206.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL97206.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL97206.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL97206.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR602326-1};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602326-1};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIL97206.1}.
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DR EMBL; AJXS01000139; EIL97206.1; -; Genomic_DNA.
DR RefSeq; WP_008210347.1; NZ_AJXS01000139.1.
DR AlphaFoldDB; I4WCL5; -.
DR PATRIC; fig|1162282.3.peg.1074; -.
DR OrthoDB; 9798864at2; -.
DR Proteomes; UP000004557; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; Cytochrome c-like domain; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR PANTHER; PTHR10266; CYTOCHROME C1; 1.
DR PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF02167; Cytochrom_C1; 2.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602326-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602326-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602326-1}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..238
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003697737"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..204
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 53
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 56
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 57
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
SQ SEQUENCE 238 AA; 26701 MW; 012C42E8B50F6C0F CRC64;
MTKRLISTIL LSFGLLLGSA SAWAEGPELP SAGNNLRDQA SLQRGAHLFF NYCVGCHSLK
YMRYSRIAQD LNLSEKDLNF TGANLGDPVA MRMSDGVAEM AFGKVPPDLS LEVGAKGTDW
VYAYLDSFYL DPKTRTGWNN VLFPNVAMPF PLSALQGEQR AVMKPGTGDV EKLELAHPGT
MTPVQYQQAM RDLVNFLDYA SEPAVMQRRR YGLWVILFLA LFTFLAWLLK KEYWKDVD
//
