ID A0A073K1C2_9BACI Unreviewed; 473 AA.
AC A0A073K1C2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-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=BAMA_18065 {ECO:0000313|EMBL:KEK20336.1};
OS Bacillus manliponensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK20336.1, ECO:0000313|Proteomes:UP000027822};
RN [1] {ECO:0000313|EMBL:KEK20336.1, ECO:0000313|Proteomes:UP000027822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK20336.1,
RC ECO:0000313|Proteomes:UP000027822};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT 1A00708).";
RL Submitted (JUN-2014) 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:KEK20336.1}.
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DR EMBL; JOTN01000004; KEK20336.1; -; Genomic_DNA.
DR RefSeq; WP_034637806.1; NZ_JOTN01000004.1.
DR AlphaFoldDB; A0A073K1C2; -.
DR STRING; 574376.BAMA_18065; -.
DR eggNOG; COG1139; Bacteria.
DR OrthoDB; 9782337at2; -.
DR Proteomes; UP000027822; 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:UP000027822};
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..293
FT /note="LUD"
FT /evidence="ECO:0000259|Pfam:PF02589"
FT DOMAIN 308..375
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|Pfam:PF13183"
FT DOMAIN 384..469
FT /note="Lactate utilization protein B C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11870"
FT BINDING 311
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 314
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 317
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 321
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 364
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 367
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 371
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 473 AA; 52628 MW; 263E225F78C35296 CRC64;
MAMKISDKKF QERVGEGIED AFMRGAVSAA QTRLHTKRLD AADELGNWEE WRELGEEIRQ
HTLENLDYYL MQLSDNVAKR GGHVFFAKTK EEAADYIQKV AKKKQAKRVI KSKSMVTEEI
GMNHALEEIG CEVVESDLGE YILQVDNDPP SHIVAPALHK NRTQIRDVFQ EKLGYDKSDD
PYEMTKFVRK MLREKFVQAE IGVTGCNFAV ANTGSLCLVT NEGNADLAMS IPKIQIAVMG
MERIVPTMEE LDVLVGLLCR SAVGQKLTSY VTVAGPIQED EVDGPEEFHL VVVDNGRSEI
LGSEFRQVLQ CIRCAACVNV CPVYRHVGGH SYGSIYSGPI GAVLTPLLGG YDDYKELPYA
STLCAACTEA CPVKIPLHEL LLKHRQVIVE QEGRAPLAEK LAMKMFSMGA SSAALYKMGS
KMAPTAMSPF TSNNRVSKGV GPLKNWTEIR EFPAPNKERF RDWYKDHKKG GSN
//
