ID   LUTB2_BACMK             Reviewed;         473 AA.
AC   A9VKN1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Lactate utilization protein B 2 {ECO:0000255|HAMAP-Rule:MF_02103};
GN   Name=lutB2 {ECO:0000255|HAMAP-Rule:MF_02103};
GN   OrderedLocusNames=BcerKBAB4_1219;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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}.
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DR   EMBL; CP000903; ABY42466.1; -; Genomic_DNA.
DR   RefSeq; WP_012260585.1; NC_010184.1.
DR   AlphaFoldDB; A9VKN1; -.
DR   STRING; 315730.BcerKBAB4_1219; -.
DR   EnsemblBacteria; ABY42466; ABY42466; BcerKBAB4_1219.
DR   KEGG; bwe:BcerKBAB4_1219; -.
DR   eggNOG; COG1139; Bacteria.
DR   HOGENOM; CLU_027059_2_0_9; -.
DR   Proteomes; UP000002154; 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..473
FT                   /note="Lactate utilization protein B 2"
FT                   /id="PRO_0000383979"
FT   DOMAIN          302..332
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   DOMAIN          351..380
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         311
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         314
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         317
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         321
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         364
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         367
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         371
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   473 AA;  52626 MW;  EFF43E744B703590 CRC64;
     MSMKISEKKF NDRVGDGIQD SFMRGAVSSA QTRLYTNRLK AADELGNWEE WRELGEQIRQ
     HTLENLDYYL MQLSENVSKR GGHVYFAKTK EDAAKYIQDV AKKKQAKKVV KSKSMVTEEI
     SMNHALEEIG CEVLESDLGE YILQVDNDPP SHIIAPALHK NRTQIRDVFK EKLGYENSDD
     PYEMTKFVRK QLREKFMDAE IGVTGCNFAV ANTGSLCLVT NEGNADLVMS IPKTQIAVMG
     MERMVPTMEE LDVLVGLLCR SAVGQKLTSY VTVAGPIQEE EVDGPEEFHL VVVDNGRSQI
     LGSEFRSILQ CIRCAACVNV CPVYRHVGGH SYGSIYSGPI GAVLTPLLGG YDDYKELPYA
     SSLCGACTEA CPVKIPLHDL LLKHRQVIVE QEGRAPLAEK LAMKMFSMGA SSAALYKMGS
     KMAPAAMSPF TSGNRVSKGV GPLKNWTDIR EFPAPSKERF RDWYKNHKKG GDK