FADF_BACSU
ID FADF_BACSU Reviewed; 705 AA.
AC P45866;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable iron-sulfur-binding oxidoreductase FadF {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305};
GN Name=fadF; Synonyms=ywjF; OrderedLocusNames=BSU37180;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP GENE NAME, AND INDUCTION.
RC STRAIN=168;
RX PubMed=17189250; DOI=10.1074/jbc.m606831200;
RA Matsuoka H., Hirooka K., Fujita Y.;
RT "Organization and function of the YsiA regulon of Bacillus subtilis
RT involved in fatty acid degradation.";
RL J. Biol. Chem. 282:5180-5194(2007).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids of
CC 14-20 carbon atoms). When LCFAs are present in the medium, they are
CC converted to long-chain acyl-CoAs, which antagonize FadR as to its
CC binding to FadR boxes on target DNA and thus derepress transcription.
CC {ECO:0000269|PubMed:17189250}.
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DR EMBL; Z49782; CAA89867.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15746.1; -; Genomic_DNA.
DR PIR; S55420; S55420.
DR RefSeq; NP_391599.1; NC_000964.3.
DR RefSeq; WP_003244084.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P45866; -.
DR IntAct; P45866; 1.
DR STRING; 224308.BSU37180; -.
DR PaxDb; P45866; -.
DR PRIDE; P45866; -.
DR EnsemblBacteria; CAB15746; CAB15746; BSU_37180.
DR GeneID; 938461; -.
DR KEGG; bsu:BSU37180; -.
DR PATRIC; fig|224308.179.peg.4028; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG2181; Bacteria.
DR InParanoid; P45866; -.
DR OMA; SGCPYCL; -.
DR PhylomeDB; P45866; -.
DR BioCyc; BSUB:BSU37180-MON; -.
DR Proteomes; UP000001570; Chromosome.
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 GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR036197; NarG-like_sf.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF103501; SSF103501; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..705
FT /note="Probable iron-sulfur-binding oxidoreductase FadF"
FT /id="PRO_0000049977"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 268..298
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 360..391
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 277
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 280
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 283
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 287
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 371
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 374
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 377
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 381
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 705 AA; 79186 MW; CE86B8F733FBB9A8 CRC64;
MSGFLIANAL LFLIVTAYAV YLFVYLVKTR LAYIKLGQKE QFDQRFKERL HAIWVNVFGQ
KKLLKDKKSG IIHVMFFYGF ILVQFGAIDF IIKGLAPGRN LSLGPVYPAF TFFQEIVTFL
ILIAVGWAFY RRYIEKLVRL KRGFKAGLVL IFIGGLMLTV LLGNGMNLIW HEHGLSWSEP
IASGIAFMLS GVGKTGAAVI FYIAWWIHLL FLLSFLVYVP QSKHAHLIAG PANVFFNRME
SAGKLEKIDF TDETKESYGA GKIEDFRQSQ LLDLYACVEC GRCTNMCPAT GTGKMLSPMD
LILRLRDHLT EKGAAVTSRS PWVPAAAFRH TRGNQLAAAS AGSGSQEAAA ALDYNPSLIG
DVITEEEIWA CTTCRNCEDQ CPVMNEHVDK IIDLRRYLVL TEGKMDSDAQ RAMTSIERQG
NPWGLNRKER ENWRDEAPDA EIPTVKEMKK EGKEFEYLFW VGSMGSYDNR SQKIAISFAK
LLNHAGVSFA ILGNKEKNSG DTPRRLGNEF LFQELAEKNI SEFEKNDVKK IVTIDPHAYN
LFKNEYPDFG FEGEVYHHTE VLAELVKNGK LRPQHPLHET ITFHDSCYLG RYNEVYDPPR
EILKAIPGVQ LVEMERSRET GMCCGAGGGL MWMEEETGNR INVARTEQAL AVNPSVISSG
CPYCLTMLGD GTKAKEAEDQ VKTYDVVELL AQSVLGADLK MGEKQ
