ID   LUTB_GEOSW              Reviewed;         475 AA.
AC   C5D586;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Lactate utilization protein B {ECO:0000255|HAMAP-Rule:MF_02103};
GN   Name=lutB {ECO:0000255|HAMAP-Rule:MF_02103}; OrderedLocusNames=GWCH70_0391;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001638; ACS23312.1; -; Genomic_DNA.
DR   RefSeq; WP_012749126.1; NC_012793.1.
DR   AlphaFoldDB; C5D586; -.
DR   STRING; 471223.GWCH70_0391; -.
DR   EnsemblBacteria; ACS23312; ACS23312; GWCH70_0391.
DR   KEGG; gwc:GWCH70_0391; -.
DR   eggNOG; COG1139; Bacteria.
DR   HOGENOM; CLU_027059_2_0_9; -.
DR   OMA; HCPVYDK; -.
DR   OrthoDB; 688908at2; -.
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.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; Repeat;
KW   Transport.
FT   CHAIN           1..475
FT                   /note="Lactate utilization protein B"
FT                   /id="PRO_0000383982"
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   475 AA;  52835 MW;  E6FD1BBB844AE866 CRC64;
     MAMKIDGANF HERVETNLHN TFMRGAVAGA QERLHTRRLE AAEELGNWEE WRALGEEIRQ
     HTLENLDYYL MQLSENVAKR GGHVFFAQTA EEANNYIRNV VIQKNAKKIV KSKSMVTEEI
     NLNAVLEAAG CEVIETDLGE YILQVDDHDP PSHIVAPALH KNKEQIRDVF RQKLGYKQTE
     KPEELALHAR KMLRHEYLTA DIGITGCNFA IAESGSITLV TNEGNADLVT ALPKTQITVM
     GMERIVPTFE EMEVLVSLLT RSAVGQKLTS YITVLTGPRD EGDVDGPEEF HLVIVDNGRS
     NILGTEFQPV LQCIRCAACV NVCPVYRHIG GHSYGSIYSG PIGAVLSPLL GGYDDYKELP
     YASSLCAACT EACPVKIPLH ELLLKHRQVI VEREGKAPIS EKLAMKAFGL GASSSFLYKL
     GSKVAPSALT PFTNDDRISK GPGPLKAWTE IREFPAPNKE RFRDWFREHQ KGGEK