RDXA_CERS4
ID RDXA_CERS4 Reviewed; 469 AA.
AC Q01854; Q3IXU2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein RdxA;
GN Name=rdxA; OrderedLocusNames=RHOS4_30740; ORFNames=RSP_3027;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400197; DOI=10.1128/jb.174.20.6444-6454.1992;
RA Neidle E.L., Kaplan S.;
RT "Rhodobacter sphaeroides rdxA, a homolog of Rhizobium meliloti fixG,
RT encodes a membrane protein which may bind cytoplasmic [4Fe-4S] clusters.";
RL J. Bacteriol. 174:6444-6454(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Predicted to be involved in a redox process.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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DR EMBL; M94725; AAA26117.1; -; Genomic_DNA.
DR EMBL; CP000144; ABA80642.1; -; Genomic_DNA.
DR PIR; A45728; A45728.
DR RefSeq; WP_011338980.1; NZ_CP030272.1.
DR RefSeq; YP_354543.1; NC_007494.2.
DR AlphaFoldDB; Q01854; -.
DR SMR; Q01854; -.
DR STRING; 272943.RSP_3027; -.
DR EnsemblBacteria; ABA80642; ABA80642; RSP_3027.
DR KEGG; rsp:RSP_3027; -.
DR PATRIC; fig|272943.9.peg.3444; -.
DR eggNOG; COG0348; Bacteria.
DR OMA; GHQAVWW; -.
DR PhylomeDB; Q01854; -.
DR Proteomes; UP000002703; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR014116; Cyt_c_oxidase_cbb3_FixG.
DR InterPro; IPR032879; FixG_C.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF13746; Fer4_18; 1.
DR Pfam; PF12801; Fer4_5; 1.
DR Pfam; PF11614; FixG_C; 1.
DR TIGRFAMs; TIGR02745; ccoG_rdxA_fixG; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..469
FT /note="Protein RdxA"
FT /id="PRO_0000159237"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..75
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..183
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..469
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 242..270
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 266..295
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 251
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 51869 MW; 1D05F128672FDC28 CRC64;
MSEPLYAPRT PIFPRQISGA FRTAKWWILA VSLGIYLLTP WLRWDRGPNL PDQAVLIDIA
GRRFFLFGIQ IWPHEFYFVA GLLIMAGLGL FLFTSAAGRV WCGYACPQTV WTDLFLLVER
RIEGDRNAQI RLHRQAWTAE KVWKRLLKWS VWAAISLLTG GAWVFYFADA PTLLNGLVTL
TAHPVAWITI FVLTATTFVF AGFMREQICI YACPWPRIQA ALMDEETITV AYRDWRGEPR
GKRSETGRGD CIDCMACVNV CPMGIDIREG QQMACITCGL CIDACDDTMD RIGRPRGLIG
YLALSDEHLE RAGDTPKPAW RRLFRLRTSL YAVLWAGVGV TLIAALLLRP AVDLAVTPVR
NPLFVTLSDG SIRNAYELRL RNMSGEDRRF RLAVDGSAGL RPSIEGSAGL DVPVAANATG
LVRLYLTAPQ GSDPATGALT DLRIRLDDAG GPEGGPVAAV KAAFHGARS
