ID G4HAK0_9BACL Unreviewed; 136 AA.
AC G4HAK0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Cytochrome c class I {ECO:0000313|EMBL:EHB66959.1};
GN ORFNames=PaelaDRAFT_1183 {ECO:0000313|EMBL:EHB66959.1};
OS Paenibacillus lactis 154.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB66959.1, ECO:0000313|Proteomes:UP000003891};
RN [1] {ECO:0000313|EMBL:EHB66959.1, ECO:0000313|Proteomes:UP000003891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154 {ECO:0000313|EMBL:EHB66959.1,
RC ECO:0000313|Proteomes:UP000003891};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA Allgaier M., Woyke T.J.;
RT "The draft genome of Paenibacillus lactis 154.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000025-1}.
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DR EMBL; AGIP01000002; EHB66959.1; -; Genomic_DNA.
DR RefSeq; WP_007128358.1; NZ_AGIP01000002.1.
DR AlphaFoldDB; G4HAK0; -.
DR STRING; 743719.PaelaDRAFT_1183; -.
DR PATRIC; fig|743719.3.peg.1181; -.
DR eggNOG; COG2010; Bacteria.
DR OrthoDB; 7933886at2; -.
DR Proteomes; UP000003891; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR012218; Cyt_c_BACSU-c550-rel.
DR InterPro; IPR008168; Cyt_C_IC.
DR PANTHER; PTHR37823; CYTOCHROME C-553-LIKE; 1.
DR PANTHER; PTHR37823:SF4; MENAQUINOL-CYTOCHROME C REDUCTASE CYTOCHROME B_C SUBUNIT; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000025; Cytc_Bsub_c550; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000025-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000025-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000025-2}; Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..136
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039484895"
FT DOMAIN 60..136
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 29..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000025-1"
FT BINDING 76
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000025-1"
FT BINDING 77
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:PIRSR000025-2"
FT BINDING 113
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:PIRSR000025-2"
SQ SEQUENCE 136 AA; 13680 MW; A32B7CF344F15EB4 CRC64;
MFKKGWFIAA LITVLVLSLA ACGGGGNNAT EPAPADGTEQ APDTANGGNA GNGEGATGGD
VSAQAQSLYN ANCMACHATD LGGGGNFPSL QKIGAEHSAE EIAGIISNGR GGMPSFKDRL
SEDDITVLSQ WLAQKK
//
