LUTB_BACSU
ID LUTB_BACSU Reviewed; 479 AA.
AC O07021;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Lactate utilization protein B;
GN Name=lutB; Synonyms=yvfW; OrderedLocusNames=BSU34040;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION IN LACTATE UTILIZATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=3610;
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 essential for L-lactate degradation and allows cells to
CC grow with lactate as the sole carbon source. Has probably a role as an
CC electron transporter during oxidation of L-lactate. May also allow
CC cells to utilize an alternative carbon source during biofilm formation,
CC since it contributes to the formation of architecturally complex
CC communities when lactate is present. {ECO:0000269|PubMed:19201793}.
CC -!- INDUCTION: Is under the dual control of the transcriptional repressors
CC LutR and SinR, which allows the lutABC operon to be induced during both
CC growth in liquid culture and biofilm formation. Is induced by L-
CC lactate, which relieves LutR repression. {ECO:0000269|PubMed:19201793}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC minimal medium with L-lactate as the sole carbon source. Cells lacking
CC the lutABC operon exhibit little or no defect in biofilm formation on
CC MSgg medium, but form small colonies that almost completely lacked
CC surface architecture when glycerol is replaced with L-lactate in the
CC MSgg medium. {ECO:0000269|PubMed:19201793}.
CC -!- SIMILARITY: Belongs to the LutB/YkgF family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15409.1; -; Genomic_DNA.
DR PIR; F70039; F70039.
DR RefSeq; NP_391284.1; NC_000964.3.
DR RefSeq; WP_003228307.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O07021; -.
DR IntAct; O07021; 1.
DR MINT; O07021; -.
DR STRING; 224308.BSU34040; -.
DR jPOST; O07021; -.
DR PaxDb; O07021; -.
DR PRIDE; O07021; -.
DR DNASU; 938159; -.
DR EnsemblBacteria; CAB15409; CAB15409; BSU_34040.
DR GeneID; 938159; -.
DR KEGG; bsu:BSU34040; -.
DR PATRIC; fig|224308.179.peg.3690; -.
DR eggNOG; COG1139; Bacteria.
DR InParanoid; O07021; -.
DR OMA; HCPVYDK; -.
DR PhylomeDB; O07021; -.
DR BioCyc; BSUB:BSU34040-MON; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..479
FT /note="Lactate utilization protein B"
FT /id="PRO_0000360418"
FT DOMAIN 304..334
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 353..382
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 313
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 53474 MW; 7C19FFF9E6F8F010 CRC64;
MAMKIGTDAF KERVSQGIDN EFMRGAVSGA QERLRTRRLE AAEELGNWEE WRSLSEEIRQ
HVLENLDFYL GQLAENVAKR GGHVYFAKTA EEASSYIRDV IQKKNGKKIV KSKSMVTEEI
NLNEVLEKEG CEVVETDLGE YILQIDDHDP PSHIVAPALH KNKEQIRDVF KERLDYQHTE
KPEELVMHAR AILRKKFLEA DIGITGCNFA IADTGSVSLV TNEGNGRLVS TLPKTQITVM
GMERIVPSFS EFEVLVSMLT RSAVGQRLTS YITALTGPKL EGEVDGPEEF HLVIVDNGRS
NILGTEFQSV LQCIRCAACI NVCPVYRHVG GHSYGSIYSG PIGAVLSPLL GGYDDYKELP
YASSLCAACS EACPVKIPLH ELLLKHRQNI VEKEGRAPIS EKLAMKAFGL GASSLSLYKM
GSKWAPAAMT PFTEDEKISK GPGPLKNWTQ IRDFPAPHKS RFRDWFADRE TSERTKEEQ
