ID C3M8I0_SINFN Unreviewed; 148 AA.
AC C3M8I0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Cytochrome c-556 {ECO:0000313|EMBL:ACP24526.1};
GN Name=cycF {ECO:0000313|EMBL:ACP24526.1};
GN OrderedLocusNames=NGR_c07330 {ECO:0000313|EMBL:ACP24526.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24526.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP24526.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR000027-2}.
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DR EMBL; CP001389; ACP24526.1; -; Genomic_DNA.
DR RefSeq; WP_012707311.1; NC_012587.1.
DR RefSeq; YP_002825279.1; NC_012587.1.
DR AlphaFoldDB; C3M8I0; -.
DR STRING; 394.NGR_c07330; -.
DR KEGG; rhi:NGR_c07330; -.
DR PATRIC; fig|394.7.peg.3549; -.
DR eggNOG; COG3909; Bacteria.
DR HOGENOM; CLU_106713_2_0_5; -.
DR OrthoDB; 9811729at2; -.
DR Proteomes; UP000001054; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..148
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002929404"
FT BINDING 136
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 /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000027-2"
FT BINDING 140
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 148 AA; 15328 MW; 83BAC00D5475F587 CRC64;
MKIRAFVLAA ALAGLGITAV TAADEPQAVR QQLMKKVGQA AGALSGIAKG EKPYDAEIVK
ASLTTISETV KVFPSHFPAG SETGSETEAS PKIWQNMDDF KAKAAKLGGD AEKILAELPA
DQAGVGAALG VLGKDCASCH ESYRLKKE
//
