ID A0A0A0HLB2_9RHOB Unreviewed; 364 AA.
AC A0A0A0HLB2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Photosynthetic reaction center cytochrome c subunit {ECO:0000256|ARBA:ARBA00015978, ECO:0000256|PIRNR:PIRNR000017};
GN ORFNames=rosmuc_03202 {ECO:0000313|EMBL:KGM86903.1};
OS Roseovarius mucosus DSM 17069.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1288298 {ECO:0000313|EMBL:KGM86903.1, ECO:0000313|Proteomes:UP000030021};
RN [1] {ECO:0000313|EMBL:KGM86903.1, ECO:0000313|Proteomes:UP000030021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17069 {ECO:0000313|EMBL:KGM86903.1,
RC ECO:0000313|Proteomes:UP000030021};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The reaction center of purple bacteria contains a tightly
CC bound cytochrome molecule which re-reduces the photo oxidized primary
CC electron donor. {ECO:0000256|ARBA:ARBA00003196,
CC ECO:0000256|PIRNR:PIRNR000017}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000256|PIRNR:PIRNR000017,
CC ECO:0000256|PIRSR:PIRSR000017-1}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGM86903.1}.
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DR EMBL; AONH01000016; KGM86903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0HLB2; -.
DR STRING; 215743.ROSMUCSMR3_00896; -.
DR PATRIC; fig|1288298.3.peg.3210; -.
DR eggNOG; ENOG502Z7SF; Bacteria.
DR HOGENOM; CLU_050380_0_0_5; -.
DR OrthoDB; 9813732at2; -.
DR Proteomes; UP000030021; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; Photosynthetic Reaction Center, subunit C, domain 2; 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 NCBIfam; NF040706; photo_cyt_PufC; 1.
DR Pfam; PF02276; CytoC_RC; 1.
DR PIRSF; PIRSF000017; RC_cytochrome; 1.
DR SUPFAM; SSF48695; Multiheme cytochromes; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|PIRNR:PIRNR000017};
KW Heme {ECO:0000256|PIRNR:PIRNR000017, ECO:0000256|PIRSR:PIRSR000017-1};
KW Iron {ECO:0000256|PIRNR:PIRNR000017, ECO:0000256|PIRSR:PIRSR000017-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000017,
KW ECO:0000256|PIRSR:PIRSR000017-2};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW ECO:0000256|PIRNR:PIRNR000017};
KW Reaction center {ECO:0000256|PIRNR:PIRNR000017};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|PIRNR:PIRNR000017}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 81..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
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:0000256|PIRSR:PIRSR000017-2"
FT BINDING 158
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:0000256|PIRSR:PIRSR000017-2"
FT BINDING 169
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000017-1"
FT BINDING 172
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000017-1"
FT BINDING 173
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:0000256|PIRSR:PIRSR000017-2"
FT BINDING 258
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:0000256|PIRSR:PIRSR000017-2"
FT BINDING 269
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000017-1"
FT BINDING 272
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000017-1"
FT BINDING 273
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:0000256|PIRSR:PIRSR000017-2"
FT BINDING 330
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000017-1"
FT BINDING 333
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000017-1"
FT BINDING 334
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:0000256|PIRSR:PIRSR000017-2"
SQ SEQUENCE 364 AA; 39533 MW; BDFAAB59A2CE9CAE CRC64;
MFPKWFDKWN RDNPTNIFGP AVAIGTVGGA VFVAALLVTW GQPYATESLQ TGPRGTGMSV
PEFKLDLAKP DPSIESFLAS TSAPVVPQGG EQTAGEAREN VPPGLEGLTV ENYDRLLAAM
RVWTGIPDLF ESVDSYQTAV GHVMIGMTQN LNEEWSGHVN ANKEVGVTCY TCHRGQPVPS
DVWFKISPVN ETVEGWSANQ NRVTVQSQYT SLPSDALEKY LLDGESIKVH DLESRVAGVP
GTDGYPGIQQ AERTYSLMNY VANSLGVNCV FCHNSRAFYD GAQVTPQWGT EILGIEMVLE
LNNTYLVPLE GLLPENRLGP VYADAPKAAC KTCHKGYQQP LQGTNVIGDW PELATTSGTP
DYSN
//
