ID LUTB_BACC1 Reviewed; 473 AA.
AC Q73BK1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Lactate utilization protein B {ECO:0000255|HAMAP-Rule:MF_02103};
GN Name=lutB {ECO:0000255|HAMAP-Rule:MF_02103}; OrderedLocusNames=BCE_1417;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS40346.1; -; Genomic_DNA.
DR AlphaFoldDB; Q73BK1; -.
DR DNASU; 2748567; -.
DR KEGG; bca:BCE_1417; -.
DR HOGENOM; CLU_027059_2_0_9; -.
DR Proteomes; UP000002527; 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; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.40.50.10420; NagB/RpiA/CoA transferase-like; 1.
DR HAMAP; MF_02103; LutB; 1.
DR InterPro; IPR004452; 4Fe-4S-bd.
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; IPR024569; LutB_C.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR NCBIfam; TIGR00273; LutB/LldF family L-lactate oxidation iron-sulfur protein; 1.
DR PANTHER; PTHR47153; LACTATE UTILIZATION PROTEIN B; 1.
DR PANTHER; PTHR47153:SF2; LACTATE UTILIZATION PROTEIN B; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR Pfam; PF02589; LUD_dom; 1.
DR Pfam; PF11870; LutB_C; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 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"
FT /id="PRO_0000383964"
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; 52669 MW; E09A2BDDA8A5822B CRC64;
MSMKISEKKF NDRVGDGIQD SFMRGAVSSA QTRLYTNRLK AADELGNWEE WRELGEEIRQ
HTLENLDYYL MQLSENVSKR GGHVYFAKTK EEAAKYIQDV AKKKQAKKVV KSKSMVTEEI
SMNHALEEIG CEVLESDLGE YILQVDNDPP SHIIAPALHK NRTQIRDVFK EKLGYENSDD
PYEMTKFVRK QLREKFMDAE IGVTGCNFAV ANTGSLCLVT NEGNADLVMS IPKTQIAVMG
MERMVPTMEE LDVLVGLLCR SAVGQKLTSY VTVAGPIQEE EVDGPEEFHL VVVDNGRSQI
LGSEFRQVLQ CIRCAACVNV CPVYRHVGGH SYGSIYSGPI GAVLTPLLGG YDDYKELPYA
SSLCGACTEA CPVKIPLHDL LLKHRQVIVE QEGRAPLAEK LAMKMFSMGA SSAALYKMGS
KMAPAAMSPF TSGNRVSKGV GPLKNWTDIR EFPAPSKERF RDWYKDHKKG GDK
//
