RNFB_CLOLD
ID RNFB_CLOLD Reviewed; 284 AA.
AC D8GR71;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Proton-translocating ferredoxin:NAD(+) oxidoreductase complex subunit B {ECO:0000305};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000269|PubMed:23269825};
DE AltName: Full=Rnf electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
GN Name=rnfB {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000312|EMBL:ADK14209.1};
GN OrderedLocusNames=CLJU_c11410 {ECO:0000312|EMBL:ADK14209.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX PubMed=23269825; DOI=10.1128/mbio.00406-12;
RA Tremblay P.L., Zhang T., Dar S.A., Leang C., Lovley D.R.;
RT "The Rnf complex of Clostridium ljungdahlii is a proton-translocating
RT ferredoxin:NAD+ oxidoreductase essential for autotrophic growth.";
RL MBio 4:E00406-E00412(2012).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane. Couples
CC electron transfer from reduced ferredoxin to NAD(+) with translocation
CC of H(+) out of the cell. Essential for energy conservation during
CC autotrophic growth. Contributes to ATP synthesis during heterotrophic
CC growth. {ECO:0000269|PubMed:23269825}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00463};
CC Note=Binds 5 [4Fe-4S] clusters. {ECO:0000305};
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00463}.
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
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; CP001666; ADK14209.1; -; Genomic_DNA.
DR RefSeq; WP_013237806.1; NZ_LITS01000015.1.
DR AlphaFoldDB; D8GR71; -.
DR STRING; 748727.CLJU_c11410; -.
DR EnsemblBacteria; ADK14209; ADK14209; CLJU_c11410.
DR KEGG; clj:CLJU_c11410; -.
DR PATRIC; fig|748727.19.peg.4231; -.
DR eggNOG; COG1148; Bacteria.
DR eggNOG; COG2878; Bacteria.
DR HOGENOM; CLU_053470_0_0_9; -.
DR OMA; MLPGANC; -.
DR OrthoDB; 1619561at2; -.
DR BRENDA; 7.1.1.11; 12866.
DR Proteomes; UP000001656; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR HAMAP; MF_00463; RsxB_RnfB; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010207; Elect_transpt_cplx_RnfB/RsxB.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF04060; FeS; 1.
DR TIGRFAMs; TIGR01944; rnfB; 1.
DR PROSITE; PS51656; 4FE4S; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Repeat; Translocase; Transport.
FT CHAIN 1..284
FT /note="Proton-translocating ferredoxin:NAD(+)
FT oxidoreductase complex subunit B"
FT /id="PRO_0000443518"
FT DOMAIN 32..92
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 133..162
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 163..192
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 206..237
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 239..269
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT REGION 1..26
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 178
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 182
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 217
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 220
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 227
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 249
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 254
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 258
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 284 AA; 29119 MW; 9E296EDE80B11EDB CRC64;
MNTVIMILVV MTIIGLIFGL VLAYVNKRFA MEVNPLVDLV EDVLPKGQCG GCGFAGCKAY
AEAVVLDESV PPNLCVPGKA AVAEQVAKLT GKSAPPIEPR VAHVRCGGDC TKAVKNFEYE
GIHDCVAANL LEGGPKACKY GCLGFGTCVK SCPFGAMAMG SNGLPIIDTD ICTGCGTCVS
ACPKQVLGFR PVGSKVMVNC NSKNKGGAVR KACSVGCLGC GLCAKNCPND AIKVENNLAV
VDQSICASCS EATCLAKCPT GAIKAIVSGT DLQQQSKNEA AANS
