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LUTB_MACCJ
ID   LUTB_MACCJ              Reviewed;         477 AA.
AC   B9E9G9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Lactate utilization protein B {ECO:0000255|HAMAP-Rule:MF_02103};
GN   Name=lutB {ECO:0000255|HAMAP-Rule:MF_02103}; OrderedLocusNames=MCCL_0173;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH16880.1; -; Genomic_DNA.
DR   RefSeq; WP_012656084.1; NC_011999.1.
DR   AlphaFoldDB; B9E9G9; -.
DR   STRING; 458233.MCCL_0173; -.
DR   EnsemblBacteria; BAH16880; BAH16880; MCCL_0173.
DR   KEGG; mcl:MCCL_0173; -.
DR   eggNOG; COG1139; Bacteria.
DR   HOGENOM; CLU_027059_2_0_9; -.
DR   OMA; HCPVYDK; -.
DR   OrthoDB; 688908at2; -.
DR   Proteomes; UP000001383; 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..477
FT                   /note="Lactate utilization protein B"
FT                   /id="PRO_0000383985"
FT   DOMAIN          304..334
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   DOMAIN          353..382
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02103"
FT   REGION          443..463
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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02103"
SQ   SEQUENCE   477 AA;  53276 MW;  8479E7A4ED8EFE7D CRC64;
     MSMRIGNETF KQAVKTELKD DFMRGAVSSA QDRLRERKLK TQEDLGNWEE WRDHSEEIRQ
     HTLANLDYYL NMLSENVAAK GGHVFFAETA EEANQYVQKV LRDKNAKKVA KSKSMVTEEI
     GLNEAMEAVG CEVIETDLGE YILQVDDHNP PSHIVVPALH LNKEQIEKVF KEKLGYDKSS
     QPEELALFAR QKLREEFLSA DVGVTGCNFG VAESGSFSLV TNEGNARMVT TLPKTQITVM
     GMERLVPTHE ELEVLVSMLT RSAVGQKLTS YVTTLTGPRA EDEIDGPEEF HLIIVDNGRS
     KILGTQFQSI LQCIRCAACV NVCPVYRQTG GHSYGSIYPG PIGAVLSPLL GGYDTYKELP
     YASTLCGACT EACPVKIPLH DLLLEHRRVI VEEEHMSPVA ERLVMKGFAQ GASHSTLFKY
     GTKAAPALMS PFENKDKGMI TKGPKPLQAW TNSRDFPMPD DENFRDWMQN RLKRGAK
 
 
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