ID J0CGF8_RHILT Unreviewed; 146 AA.
AC J0CGF8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Cytochrome c556 {ECO:0000313|EMBL:EJC78460.1};
GN ORFNames=Rleg4DRAFT_0027 {ECO:0000313|EMBL:EJC78460.1};
OS Rhizobium leguminosarum bv. trifolii WSM2297.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=754762 {ECO:0000313|EMBL:EJC78460.1, ECO:0000313|Proteomes:UP000005732};
RN [1] {ECO:0000313|EMBL:EJC78460.1, ECO:0000313|Proteomes:UP000005732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2297 {ECO:0000313|EMBL:EJC78460.1,
RC ECO:0000313|Proteomes:UP000005732};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R.,
RA O'Hara G., Rui T., Howieson J., Reeve W., Woyke T.;
RT "Improved High-Quality Draft Sequence of Rhizobium leguminosarum bv.
RT trifolii WSM2297.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR000027-2}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH719395; EJC78460.1; -; Genomic_DNA.
DR AlphaFoldDB; J0CGF8; -.
DR HOGENOM; CLU_106713_2_0_5; -.
DR OrthoDB; 9811729at2; -.
DR Proteomes; UP000005732; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
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 Gene3D; 1.20.120.10; Cytochrome c/b562; 1.
DR InterPro; IPR010980; Cyt_c/b562.
DR InterPro; IPR002321; Cyt_c_II.
DR InterPro; IPR012127; Cyt_c_prime.
DR InterPro; IPR015984; Cyt_c_prime_subgr.
DR Pfam; PF01322; Cytochrom_C_2; 1.
DR PIRSF; PIRSF000027; Cytc_c_prime; 1.
DR PRINTS; PR00608; CYTCHROMECII.
DR SUPFAM; SSF47175; Cytochromes; 1.
DR PROSITE; PS51009; CYTCII; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000027-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000027-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000027-1}; Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..146
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003732313"
FT BINDING 135
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT BINDING 138
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT BINDING 139
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:0000256|PIRSR:PIRSR000027-1"
SQ SEQUENCE 146 AA; 14884 MW; 84511D05773A304D CRC64;
MNWKAVAAAA AMAGIAFGSV TAADGTHDSR IALMKQIGGS AGALAAIAKG TKPYDAEAVK
AALTTIATTA KVFPDQFKPG TETGDKEASP KIWENMDDFK ARAAKLSTDA ETALAQLPAD
PAAVGATMNT LGANCAGCHK AYRIKE
//
