ID G2FDU5_9GAMM Unreviewed; 246 AA.
AC G2FDU5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cytochrome c1 {ECO:0000313|EMBL:EGW54929.1};
GN Name=petC {ECO:0000313|EMBL:EGW54929.1};
GN ORFNames=TevJSym_ag00070 {ECO:0000313|EMBL:EGW54929.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW54929.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW54929.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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:EGW54929.1}.
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DR EMBL; AFZB01000007; EGW54929.1; -; Genomic_DNA.
DR RefSeq; WP_005961930.1; NZ_AFZB01000007.1.
DR AlphaFoldDB; G2FDU5; -.
DR PATRIC; fig|1049564.3.peg.1078; -.
DR eggNOG; COG2857; Bacteria.
DR Proteomes; UP000005167; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..246
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003429407"
FT TRANSMEM 219..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..205
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 50
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
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 54
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
SQ SEQUENCE 246 AA; 27873 MW; E418DE7C03EF5F9D CRC64;
MKKLFFAFLL AAAPLMGFAS GGGVHLDDAD IDLSDEASLQ RGAKYFVNYC LSCHSAKFQR
YNRMARDLGL TEEEVKQNLM FTTDKIGNTM TIAMPQEQAE AWFGTAPPDL SVIARARGVD
WLYTYFRSFY VDESRPFGVN NIVFPDVGMP HVLWELQGPQ KAVFRTEQDA AGNETHVFDK
FEQIAPGKLS PGEYDDVARD LTAFLSYVGE PIQMKRKSMG IWVLLFIAAF FGLAYMLKKE
YWKDVH
//
