C554_CHLAA
ID C554_CHLAA Reviewed; 414 AA.
AC P33325; A9WEY6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytochrome c-554;
DE AltName: Full=Cytochrome c554;
DE Flags: Precursor;
GN Name=puf2C; OrderedLocusNames=Caur_2089;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 308-331 AND
RP 370-400.
RX PubMed=1660302; DOI=10.1021/bi00112a012;
RA Dracheva S., Williams J.C., van Driessche G., van Beeumen J.J.,
RA Blankenship R.E.;
RT "The primary structure of cytochrome c-554 from the green photosynthetic
RT bacterium Chloroflexus aurantiacus.";
RL Biochemistry 30:11451-11458(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RX PubMed=7535995; DOI=10.1007/bf00381786;
RA Watanabe Y., Feick R.G., Shiozawa J.A.;
RT "Cloning and sequencing of the genes encoding the light-harvesting B806-866
RT polypeptides and initial studies on the transcriptional organization of
RT puf2B, puf2A and puf2C in Chloroflexus aurantiacus.";
RL Arch. Microbiol. 163:124-130(1995).
CC -!- FUNCTION: Serves as the immediate electron donor to the oxidized BChl2
CC (bacteriochlorophyll dimer) that is oxidized in the first step of
CC light-induced charge separation. Can also oxidize low-potential
CC substrates.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 4 heme groups per subunit.
CC -!- PTM: The N-terminus is blocked. {ECO:0000305}.
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; M77813; AAA23100.1; -; Genomic_DNA.
DR EMBL; CP000909; ABY35301.1; -; Genomic_DNA.
DR EMBL; X73899; CAA52106.1; -; Genomic_DNA.
DR PIR; A39303; A39303.
DR RefSeq; WP_012257955.1; NC_010175.1.
DR RefSeq; YP_001635690.1; NC_010175.1.
DR AlphaFoldDB; P33325; -.
DR STRING; 324602.Caur_2089; -.
DR EnsemblBacteria; ABY35301; ABY35301; Caur_2089.
DR KEGG; cau:Caur_2089; -.
DR PATRIC; fig|324602.8.peg.2369; -.
DR eggNOG; ENOG502Z7SF; Bacteria.
DR HOGENOM; CLU_675859_0_0_0; -.
DR OMA; YCHNIAN; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030077; C:plasma membrane light-harvesting complex; 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 GO; GO:0019684; P:photosynthesis, light reaction; IEA:InterPro.
DR CDD; cd09224; CytoC_RC; 1.
DR Gene3D; 1.10.468.10; -; 2.
DR InterPro; IPR023119; Multihaem_cyt_PRC_cyt_su-like.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR003158; Photosyn_RC_cyt_c-su.
DR Pfam; PF02276; CytoC_RC; 2.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Photosynthesis; Reference proteome; Signal; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..414
FT /note="Cytochrome c-554"
FT /id="PRO_0000006542"
FT BINDING 110
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:1660302"
FT BINDING 381
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:1660302"
FT BINDING 382
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 414 AA; 45594 MW; EA15728E99DD586D CRC64;
MQSSRPSDRQ LAIVVSVAVG IVVAVITTAT FWWVYDLTLG RAQREAAQTA GARWSPSDGI
KVITSSPPVT PTDGRQNWMG TQAWNEGVQA GQAWIQQYPN TVNVQVLIGM SSAQIWTYMQ
QYVSGALGVG CQYCHNINNF ASDEYPQKIA ARNMLRLVRD VNAEFIVNLP NWQGNYVQCA
TCHNNAPNNL EGFGAQFINS VPPIKVTVDP LDANGMAILD PAQKPEAIRE PVLLKDAILF
YIYNYQVWKP FDPNDPESGR GSLALTYDGG RTQDQVTINQ NVMNYQAWSL GVGCTFCHNS
RNFVAYELNP AGDNVLNPLY AYNKLKAQRM LLLTTWLAEN WPRYGAIAKP EIPTGSGAAS
RYSYQRLGDG QIYNVPGCYT CHQGNNIPLA SINQANIPSG DAGIVVLPPQ IRGR
