MIOC_ECOLI
ID MIOC_ECOLI Reviewed; 147 AA.
AC P03817; Q2M860;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein MioC;
GN Name=mioC; Synonyms=yieB; OrderedLocusNames=b3742, JW3720;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6357950; DOI=10.1016/0378-1119(83)90087-2;
RA Buhk H.-J., Messer W.;
RT "The replication origin region of Escherichia coli: nucleotide sequence and
RT functional units.";
RL Gene 24:265-279(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=370833; DOI=10.1073/pnas.76.2.580;
RA Meijer M., Beck E., Hansen F.G., Bergmans H.E.N., Messer W., Meyenburg K.,
RA Schaller H.;
RT "Nucleotide sequence of the origin of replication of the Escherichia coli
RT K-12 chromosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:580-584(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6169112; DOI=10.1016/s0079-6603(08)60393-1;
RA Hirota Y., Yamada M., Nishimura A., Oka A., Sugimoto K., Asada K.,
RA Takanami M.;
RT "The DNA replication origin (ori) of Escherichia coli: structure and
RT function of the ori-containing DNA fragment.";
RL Prog. Nucleic Acid Res. Mol. Biol. 26:33-48(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-147.
RC STRAIN=K12;
RX PubMed=370832; DOI=10.1073/pnas.76.2.575;
RA Sugimoto K., Oka A., Sugisaki H., Takanami M., Nishimura A., Yasuda Y.,
RA Hirota Y.;
RT "Nucleotide sequence of Escherichia coli K-12 replication origin.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:575-579(1979).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 140-147.
RX PubMed=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [9]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [10]
RP MUTAGENESIS.
RC STRAIN=K12;
RX PubMed=1620598; DOI=10.1093/nar/20.12.3029;
RA Lobner-Olesen A., Boye E.;
RT "Different effects of mioC transcription on initiation of chromosomal and
RT minichromosomal replication in Escherichia coli.";
RL Nucleic Acids Res. 20:3029-3036(1992).
RN [11]
RP PROTEIN SEQUENCE OF 2-11, AND CHARACTERIZATION.
RX PubMed=10913144; DOI=10.1074/jbc.m004497200;
RA Birch O.M., Hewitson K.S., Fuhrmann M., Burgdorf K., Baldwin J.E.,
RA Roach P.L., Shaw N.M.;
RT "MioC is an FMN-binding protein that is essential for Escherichia coli
RT biotin synthase activity in vitro.";
RL J. Biol. Chem. 275:32277-32280(2000).
CC -!- FUNCTION: Probable electron transporter required for biotin synthase
CC activity.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the flavodoxin family. MioC subfamily.
CC {ECO:0000305}.
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DR EMBL; K00826; AAA24251.1; -; Genomic_DNA.
DR EMBL; V00308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J01657; AAA24247.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L10328; AAA62094.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76765.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77546.1; -; Genomic_DNA.
DR EMBL; X01631; CAA25772.1; -; Genomic_DNA.
DR PIR; G65177; QQEC16.
DR RefSeq; NP_418198.1; NC_000913.3.
DR RefSeq; WP_000763724.1; NZ_SSZK01000036.1.
DR RefSeq; YP_006952151.1; NC_019049.1.
DR PDB; 2HNA; NMR; -; A=1-147.
DR PDB; 2HNB; NMR; -; A=1-147.
DR PDBsum; 2HNA; -.
DR PDBsum; 2HNB; -.
DR AlphaFoldDB; P03817; -.
DR SMR; P03817; -.
DR BioGRID; 4263259; 228.
DR BioGRID; 852551; 4.
DR IntAct; P03817; 4.
DR STRING; 511145.b3742; -.
DR jPOST; P03817; -.
DR PaxDb; P03817; -.
DR PRIDE; P03817; -.
DR EnsemblBacteria; AAC76765; AAC76765; b3742.
DR EnsemblBacteria; BAE77546; BAE77546; BAE77546.
DR GeneID; 948249; -.
DR KEGG; ecj:JW3720; -.
DR KEGG; eco:b3742; -.
DR PATRIC; fig|1411691.4.peg.2958; -.
DR EchoBASE; EB1185; -.
DR eggNOG; COG0716; Bacteria.
DR HOGENOM; CLU_051402_4_1_6; -.
DR InParanoid; P03817; -.
DR OMA; ACFGSGD; -.
DR PhylomeDB; P03817; -.
DR BioCyc; EcoCyc:EG11199-MON; -.
DR EvolutionaryTrace; P03817; -.
DR PRO; PR:P03817; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0051302; P:regulation of cell division; IMP:EcoCyc.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Flavoprotein;
KW FMN; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10913144, ECO:0000269|Ref.9"
FT CHAIN 2..147
FT /note="Protein MioC"
FT /id="PRO_0000196572"
FT DOMAIN 4..143
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT CONFLICT 56..99
FT /note="THGAGDIPDNLSPFYEALQEQKPDLSAVRFGAIGIGSREYDTFC -> PTVP
FT EIFRTTFLLSMKHCRNRSPIFLQSALAQSVLAVVNMTPFV (in Ref. 3;
FT AAA24247)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2HNA"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2HNB"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:2HNA"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:2HNA"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2HNB"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:2HNA"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:2HNA"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:2HNA"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2HNA"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2HNA"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2HNA"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:2HNA"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2HNB"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2HNB"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:2HNA"
SQ SEQUENCE 147 AA; 15808 MW; 48D984FFFB348730 CRC64;
MADITLISGS TLGGAEYVAE HLAEKLEEAG FTTETLHGPL LEDLPASGIW LVISSTHGAG
DIPDNLSPFY EALQEQKPDL SAVRFGAIGI GSREYDTFCG AIDKLEAELK NSGAKQTGET
LKINILDHDI PEDPAEEWLG SWVNLLK
