ID A0A0M2PGK9_9BACI Unreviewed; 474 AA.
AC A0A0M2PGK9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Lactate utilization protein B {ECO:0000256|HAMAP-Rule:MF_02103};
GN Name=lutB {ECO:0000256|HAMAP-Rule:MF_02103};
GN ORFNames=WQ54_22420 {ECO:0000313|EMBL:KKI89903.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI89903.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI89903.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI89903.1,
RC ECO:0000313|Proteomes:UP000034887};
RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) 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:KKI89903.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LATZ01000120; KKI89903.1; -; Genomic_DNA.
DR RefSeq; WP_046587554.1; NZ_LATZ01000120.1.
DR AlphaFoldDB; A0A0M2PGK9; -.
DR PATRIC; fig|1455638.3.peg.4938; -.
DR OrthoDB; 9782337at2; -.
DR Proteomes; UP000034887; 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.
DR PROSITE; PS51379; 4FE4S_FER_2; 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};
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 303..334
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 435..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 474 AA; 52841 MW; 838112825FD1A487 CRC64;
MAMKISDDKF FERVDKGVHN TFMRNAVVAA QERMQGRRLA AAEELGNWEE WRKLGEEIRT
HTLENLDYYL EQLSENVTKR GGHVFFASTK EEANEYISKV VKEKQAKKVV KSKSMVTEEI
HLNAALENAG CEVIETDLGE YILQLDDHDP PSHIVVPALH KNKEQIRDTF KEKRGYDKSE
IPEELALFAR EQLRQEFLTA DLGITGCNFA VAESGSISLV TNEGNAGLVT ALPKTQITVM
GMERIVPTWE ELDILVSLLC RSSVGQKLTS YITGLTGPKD EEDVDGPEEF HLVIVDNGRS
NILGTEFQSA LHCIRCAACV NVCPVYRHIG GHSYGSIYAG PIGAVLTPLL GGYEDYKELP
YASSLCAACT EACPVKIPLH ELLIKHRRKI VEDEKKSPFA EKLAMKGYQL AASSPSIYKA
GTKSASTVMA PFTQANSIQK GPGPMKPWTD VRDFPAPSKE RFRDWYKKRE KGGE
//
