ID A0A366XZI4_9BACI Unreviewed; 476 AA.
AC A0A366XZI4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Lactate utilization protein B {ECO:0000256|HAMAP-Rule:MF_02103};
GN Name=lutB {ECO:0000256|HAMAP-Rule:MF_02103};
GN ORFNames=DS031_10105 {ECO:0000313|EMBL:RBW69574.1};
OS Bacillus taeanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=273032 {ECO:0000313|EMBL:RBW69574.1, ECO:0000313|Proteomes:UP000253314};
RN [1] {ECO:0000313|EMBL:RBW69574.1, ECO:0000313|Proteomes:UP000253314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030017 {ECO:0000313|EMBL:RBW69574.1,
RC ECO:0000313|Proteomes:UP000253314};
RA Liu R., Huang Z.;
RT "Lottiidibacillus patelloidae gen. nov., sp. nov., isolated from the
RT intestinal tract of a marine limpet and the reclassification of B.
RT taeanensis BH030017T, B. algicola KMM 3737T and B. hwajinpoensis SW-72T as
RT genus Lottiidibacillus.";
RL Submitted (JUL-2018) 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:0000256|HAMAP-
CC Rule:MF_02103}.
CC -!- SIMILARITY: Belongs to the LutB/YkgF family. {ECO:0000256|HAMAP-
CC Rule:MF_02103}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBW69574.1}.
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DR EMBL; QOCW01000009; RBW69574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366XZI4; -.
DR OrthoDB; 9782337at2; -.
DR Proteomes; UP000253314; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_02103};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_02103};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02103};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_02103};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02103}; Reference proteome {ECO:0000313|Proteomes:UP000253314};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_02103};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_02103}.
FT DOMAIN 71..295
FT /note="LUD"
FT /evidence="ECO:0000259|Pfam:PF02589"
FT DOMAIN 310..377
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|Pfam:PF13183"
FT DOMAIN 384..471
FT /note="Lactate utilization protein B C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11870"
FT BINDING 313
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_02103"
SQ SEQUENCE 476 AA; 52795 MW; A4A1FAB9602EEFDB CRC64;
MAMKIGTEGF KERVDNGINN TFMRGAVAGA QERLSTRRID STEELGNWEE WRNLGEEIRQ
HTLENLDYYL MQFSEKVAER GGHVFFAETP DEANEYIKNV IQKKNGKKVV KSKSMVTEEI
NMNACLEEQG CEVIETDLGE YILQVDDHDP PSHIVTPALH KNKEQIRDVF KEKLAYTKTE
KPEELALHAR EMLRKEFLAA DIGITGCNFA IAESGSISLV TNEGNARLVS SLPKTQITVM
GMERIVPTFA EFEVLVSLLT RSAVGQKLTS YVTALTGPKQ EGDVDGPEEF HVVIVDNGRS
KIIGTEFQSI LQCIRCAACV NVCPIYRHVG GHSYGSIYSG PIGAVLSPLL GGYEDYKELP
YASTLCGACT DVCPVKIPLH ELLHKHRQVI VEREGKAPIS EKLAMKAFGL GSASPSLYNL
GSKLSPTAMN PFTVNNKISK GPGPLKAWTD IREFPAPDKE RFRDWFKKRG KGGVKS
//
