CY553_SPOPA
ID CY553_SPOPA Reviewed; 92 AA.
AC P82599;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytochrome c-553;
DE AltName: Full=Cytochrome c553;
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474;
RN [1]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX PubMed=10529373; DOI=10.1006/bbrc.1999.1359;
RA Vandenberghe I.H.M., Guisez Y., Ciurli S., Benini S., Van Beeumen J.J.;
RT "Cytochrome c-553 from the alkalophilic bacterium Bacillus pasteurii has
RT the primary structure characteristics of a lipoprotein.";
RL Biochem. Biophys. Res. Commun. 264:380-387(1999).
CC -!- FUNCTION: Natural electron acceptor for a formate dehydrogenase.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Note=May be released from the membrane upon cell disruption resulting
CC in an abundant soluble form of the protein.
CC -!- PTM: Is a lipoprotein in vivo.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- MASS SPECTROMETRY: Mass=9608.9; Mass_error=0.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10529373};
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR PDB; 1B7V; X-ray; 1.70 A; A=22-92.
DR PDB; 1C75; X-ray; 0.97 A; A=22-92.
DR PDB; 1K3G; NMR; -; A=22-92.
DR PDB; 1K3H; NMR; -; A=22-92.
DR PDB; 1N9C; NMR; -; A=22-92.
DR PDBsum; 1B7V; -.
DR PDBsum; 1C75; -.
DR PDBsum; 1K3G; -.
DR PDBsum; 1K3H; -.
DR PDBsum; 1N9C; -.
DR AlphaFoldDB; P82599; -.
DR SMR; P82599; -.
DR DrugBank; DB03317; Ferroheme C.
DR EvolutionaryTrace; P82599; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma 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:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 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 Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000025; Cytc_Bsub_c550; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Electron transport;
KW Heme; Iron; Lipoprotein; Membrane; Metal-binding; Transport.
FT CHAIN 1..92
FT /note="Cytochrome c-553"
FT /id="PRO_0000108403"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 35
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 36
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:0000255|PROSITE-ProRule:PRU00433"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:1C75"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1C75"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1C75"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1C75"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:1C75"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:1C75"
SQ SEQUENCE 92 AA; 8991 MW; EE69F659E7874C7F CRC64;
GGGNDTSNET DTGTSGGETA AVDAEAVVQQ KCISCHGGDL TGASAPAIDK AGANYSEEEI
LDIILNGQGG MPGGIAKGAE AEAVAAWLAE KK
