ID   LUTB_BACVZ              Reviewed;         476 AA.
AC   A7Z901;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Lactate utilization protein B {ECO:0000255|HAMAP-Rule:MF_02103};
GN   Name=lutB {ECO:0000255|HAMAP-Rule:MF_02103}; Synonyms=yvfW;
GN   OrderedLocusNames=RBAM_031460;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
CC   -!- FUNCTION: Is involved in L-lactate degradation and allows cells to grow
CC       with lactate as the sole carbon source. Has probably a role as an
CC       electron transporter during oxidation of L-lactate. {ECO:0000255|HAMAP-
CC       Rule:MF_02103}.
CC   -!- SIMILARITY: Belongs to the LutB/YkgF family. {ECO:0000255|HAMAP-
CC       Rule:MF_02103}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABS75477.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000560; ABS75477.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_007407375.1; NC_009725.2.
DR   AlphaFoldDB; A7Z901; -.
DR   STRING; 326423.RBAM_031460; -.
DR   EnsemblBacteria; ABS75477; ABS75477; RBAM_031460.
DR   GeneID; 66323451; -.
DR   KEGG; bay:RBAM_031460; -.
DR   HOGENOM; CLU_027059_2_0_9; -.
DR   Proteomes; UP000001120; Chromosome.
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:0019516; P:lactate oxidation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.40.50.10420; -; 1.
DR   HAMAP; MF_02103; LutB; 1.
DR   InterPro; IPR004452; 4Fe-4S-bd.
DR   InterPro; IPR024569; 4Fe-4S-bd_C.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR024185; FTHF_cligase-like_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR003741; LUD_dom.
DR   InterPro; IPR022825; LutB.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR47153; PTHR47153; 1.
DR   Pfam; PF11870; DUF3390; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   Pfam; PF02589; LUD_dom; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00273; TIGR00273; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; Repeat;
KW   Transport.
FT   CHAIN           1..476
FT                   /note="Lactate utilization protein B"
FT                   /id="PRO_0000383958"
FT   DOMAIN          304..334
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   DOMAIN          353..382
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         313
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         316
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         319
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         323
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         366
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         369
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         373
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
SQ   SEQUENCE   476 AA;  53132 MW;  8373E92BD8D52AF1 CRC64;
     MAMKIGTAAF KERVSEGIDN EFMRGAVSGA QERLRTRRLQ AAEELGNWED WRSHAEEIRQ
     HVLDNLDFYL EQLAENVANR GGHVFFAETA EEASSYIRDV IRQKNAKKIV KSKSMVTEEI
     NMNEVLEEEG CEVTETDLGE YILQIDDHDP PSHIVAPALH KNKEQIRDVF KERLEYKQTE
     KPEELVMHAR SVLRKKFLEA DVGITGCNFA IADTGSVSLV TNEGNGRLVS ALPKTQITVM
     GMERIVPSFS EFEVLVSMLT RSAVGQRLTS YITALTGPRQ QGEADGPEEF HLVVVDNGRS
     RILGTEFQSV LQCIRCAACI NVCPVYRHVG GHSYGSIYSG PIGAVLSPLL GGYDEYKELP
     YASSLCAACT EACPVKIPLH ELLLKHRQNI VEKEGKAPIS EKLAMKAFGL GSSSPSLYKM
     GSKWAPAAMT PFTEDDKISK GPGPLKEWTA IRDFPAPHKS RFRDWFKDRE KQKGEE