ID   LUTB_BACP2              Reviewed;         473 AA.
AC   A8FDN5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Lactate utilization protein B {ECO:0000255|HAMAP-Rule:MF_02103};
GN   Name=lutB {ECO:0000255|HAMAP-Rule:MF_02103}; Synonyms=yvfW;
GN   OrderedLocusNames=BPUM_1673;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV62352.1; -; Genomic_DNA.
DR   RefSeq; WP_012010084.1; NZ_VEIS01000012.1.
DR   AlphaFoldDB; A8FDN5; -.
DR   STRING; 315750.BPUM_1673; -.
DR   PRIDE; A8FDN5; -.
DR   EnsemblBacteria; ABV62352; ABV62352; BPUM_1673.
DR   KEGG; bpu:BPUM_1673; -.
DR   eggNOG; COG1139; Bacteria.
DR   HOGENOM; CLU_027059_2_0_9; -.
DR   OMA; HCPVYDK; -.
DR   OrthoDB; 688908at2; -.
DR   Proteomes; UP000001355; 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_0000383976"
FT   DOMAIN          303..333
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   DOMAIN          352..381
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   BINDING         312
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         315
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         318
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         322
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         365
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         368
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         372
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;  52485 MW;  78DA6C42BCCF4AC5 CRC64;
     MSMKIGAKAF KERIGEGLED TVMRGAVSSA QERLYERRLS ASEELGNWEK WRELGEEIRQ
     HTLAHLDDYL YQLSESVSAR GGHVFFAKTK EEASAYIQHV AQKKEAKKIV KSKSMVTEEI
     EMNQALEEIG CEVVESDLGE YILQVDDHEP PSHIVAPALH MTKEQIREVF HEKLGYEMSE
     TPEDMTSFVR AILREKFLEA DMGVTGCNFA VANTGSICLV TNEGNADLVT AIPKTHIAVM
     GMERMVPTME ELDVLVGLLC RSAVGQKLTS YISVVGPKGE EEVDGPEEFH LVIVDNGRSN
     ILGTAFQPVL QCIRCAACIN VCPVYRHVGG HSYGSIYPGP IGAVLSPLLG GYDDYQELPF
     ASSLCAACTD ACPVKIPLHE LLIKHRQVIV EKEGRAPKAE MMAMKMFGMG ASTPGMYQFG
     TKAAPLLMNR MASNGQISKG IGPLKNWTDI RDLPAPSKER FRDWFKKRQK EEQ