LUTB_BACCR
ID LUTB_BACCR Reviewed; 473 AA.
AC Q81GA4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Lactate utilization protein B {ECO:0000255|HAMAP-Rule:MF_02103};
GN Name=lutB {ECO:0000255|HAMAP-Rule:MF_02103}; OrderedLocusNames=BC_1304;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP FUNCTION BY COMPLEMENTATION OF B.SUBTILIS LUTABC OPERON.
RX PubMed=19201793; DOI=10.1128/jb.01464-08;
RA Chai Y., Kolter R., Losick R.;
RT "A widely conserved gene cluster required for lactate utilization in
RT Bacillus subtilis and its involvement in biofilm formation.";
RL J. Bacteriol. 191:2423-2430(2009).
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, ECO:0000269|PubMed:19201793}.
CC -!- SIMILARITY: Belongs to the LutB/YkgF family. {ECO:0000255|HAMAP-
CC Rule:MF_02103}.
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DR EMBL; AE016877; AAP08287.1; -; Genomic_DNA.
DR RefSeq; NP_831086.1; NC_004722.1.
DR RefSeq; WP_000061930.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81GA4; -.
DR STRING; 226900.BC_1304; -.
DR EnsemblBacteria; AAP08287; AAP08287; BC_1304.
DR GeneID; 67506008; -.
DR KEGG; bce:BC1304; -.
DR PATRIC; fig|226900.8.peg.1277; -.
DR HOGENOM; CLU_027059_2_0_9; -.
DR OMA; HCPVYDK; -.
DR Proteomes; UP000001417; 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;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..473
FT /note="Lactate utilization protein B"
FT /id="PRO_0000383971"
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; 52627 MW; 6286C61DFDA81864 CRC64;
MSMKISEKKF NDRVGDGIQD SFMRGAVSSA QTRLYTNRLK AADELGNWEE WRELGEQIRQ
HTLENLDYYL MQLSENVSKR GGHVYFAKTK EEAAKYIQDV AKKKQAKKVV KSKSMVTEEI
SMNHALEEIG CEVLESDLGE YILQVDNDPP SHIIAPALHK NRTQIRDVFK EKLGYENSDD
PYEMTKFVRK QLREKFMDAE IGVTGCNFAV ANTGSLCLVT NEGNADLVMS IPKTQIAVMG
MERMVPTMEE LDVLVGLLCR SAVGQKLTSY VTVAGPIQEE EVDGPEEFHL VVVDNGRSQI
LGSEFRSVLQ CIRCAACVNV CPVYRHVGGH SYGSIYSGPI GAVLTPLLGG YDDYKELPYA
SSLCGACTEA CPVKIPLHDL LLKHRQVIVE QEGRAPLAEK LAMKMFSMGA SSAALYKMGS
KMAPAAMSPF TSGNRVSKGV GPLKNWTDIR EFPAPSKERF RDWYKDHKKG GDK
