GenomeNet

Database: UniProt
Entry: F3ZVJ3_MAHA5
LinkDB: F3ZVJ3_MAHA5
Original site: F3ZVJ3_MAHA5 
ID   F3ZVJ3_MAHA5            Unreviewed;       276 AA.
AC   F3ZVJ3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000256|HAMAP-Rule:MF_00463};
DE            EC=7.-.-.- {ECO:0000256|HAMAP-Rule:MF_00463};
DE   AltName: Full=Rnf electron transport complex subunit B {ECO:0000256|HAMAP-Rule:MF_00463};
GN   Name=rnfB {ECO:0000256|HAMAP-Rule:MF_00463};
GN   OrderedLocusNames=Mahau_1158 {ECO:0000313|EMBL:AEE96355.1};
OS   Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family IV. Incertae Sedis; Mahella.
OX   NCBI_TaxID=697281 {ECO:0000313|EMBL:AEE96355.1, ECO:0000313|Proteomes:UP000008457};
RN   [1] {ECO:0000313|Proteomes:UP000008457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC   {ECO:0000313|Proteomes:UP000008457};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Pukall R.,
RA   Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Mahella australiensis DSM 15567.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEE96355.1, ECO:0000313|Proteomes:UP000008457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC   {ECO:0000313|Proteomes:UP000008457};
RX   PubMed=21886860;
RA   Sikorski J., Teshima H., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M.,
RA   Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Ngatchou-Djao O.D., Rohde M.,
RA   Pukall R., Spring S., Abt B., Goker M., Detter J.C., Woyke T., Bristow J.,
RA   Markowitz V., Hugenholtz P., Eisen J.A., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Mahella australiensis type strain (50-1
RT   BON).";
RL   Stand. Genomic Sci. 4:331-341(2011).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00463};
CC       Note=Binds 3 [4Fe-4S] clusters. {ECO:0000256|HAMAP-Rule:MF_00463};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC       RnfD, RnfE and RnfG. {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|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; CP002360; AEE96355.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3ZVJ3; -.
DR   STRING; 697281.Mahau_1158; -.
DR   KEGG; mas:Mahau_1158; -.
DR   eggNOG; COG2768; Bacteria.
DR   eggNOG; COG2878; Bacteria.
DR   HOGENOM; CLU_053470_0_0_9; -.
DR   Proteomes; UP000008457; 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   CDD; cd10549; MtMvhB_like; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 1.10.15.40; Electron transport complex subunit B, putative Fe-S cluster; 1.
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   NCBIfam; TIGR01944; rnfB; 1.
DR   PANTHER; PTHR43560; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR   PANTHER; PTHR43560:SF1; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR   Pfam; PF13187; Fer4_9; 2.
DR   Pfam; PF04060; FeS; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
DR   PROSITE; PS51656; 4FE4S; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 3.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00463};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00463};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00463};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00463, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00463}; Reference proteome {ECO:0000313|Proteomes:UP000008457};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00463}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..93
FT                   /note="4Fe-4S"
FT                   /evidence="ECO:0000259|PROSITE:PS51656"
FT   DOMAIN          163..192
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          206..236
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          237..266
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..28
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         59
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         139
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         143
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         149
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         153
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00463"
SQ   SEQUENCE   276 AA;  28324 MW;  8A17BA828DDB5675 CRC64;
     MNINDILIPV VTLGGLGLIF GAILAFASSR FAVEKDPRVD EVREALPGAN CGACGYPGCD
     GLAAAIVAGK APVNACTVGG AASAEKIGAI MGVEAQAGEK QVARVLCQGD LEAAAQKYKY
     VGIESCAAAN ALGGGSKACG YGCLGFGDCV KACPFDAIDI VNGVAIVDEK RCTGCTICVA
     ACPKGIIQMV PQSKRVVILC ASLDKGKLVR GYCKVGCIAC NICVRKCPEN AIVLENNLAH
     IVYDKCTNCA ECVDKCPAST IKNYDGVCEE RETAAL
//
DBGET integrated database retrieval system