SBMC_ECOLI
ID SBMC_ECOLI Reviewed; 157 AA.
AC P33012;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DNA gyrase inhibitor;
GN Name=sbmC; Synonyms=gyrI, yeeB; OrderedLocusNames=b2009, JW1991;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=RYC1000;
RX PubMed=8709849; DOI=10.1111/j.1365-2958.1995.mmi_18020301.x;
RA Baquero M.-R., Bouzon M., Varea J., Moreno F.;
RT "sbmC, a stationary-phase induced SOS Escherichia coli gene, whose product
RT protects cells from the DNA replication inhibitor microcin B17.";
RL Mol. Microbiol. 18:301-311(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 1-16, FUNCTION, AND CHARACTERIZATION.
RX PubMed=9442027; DOI=10.1074/jbc.273.4.1933;
RA Nakanishi A., Oshida T., Matsushita T., Imajoh-Ohmi S., Ohnuki T.;
RT "Identification of DNA gyrase inhibitor (GyrI) in Escherichia coli.";
RL J. Biol. Chem. 273:1933-1938(1998).
RN [7]
RP FUNCTION.
RX PubMed=11850398; DOI=10.1093/embo-reports/kvf038;
RA Chatterji M., Nagaraja V.;
RT "GyrI: a counter-defensive strategy against proteinaceous inhibitors of DNA
RT gyrase.";
RL EMBO Rep. 3:261-267(2002).
RN [8]
RP INTERACTION WITH DNA GYRASE.
RX PubMed=11777918; DOI=10.1074/jbc.m111278200;
RA Nakanishi A., Imajoh-Ohmi S., Hanaoka F.;
RT "Characterization of the interaction between DNA gyrase inhibitor and DNA
RT gyrase of Escherichia coli.";
RL J. Biol. Chem. 277:8949-8954(2002).
RN [9]
RP FUNCTION.
RX PubMed=13680098; DOI=10.1007/s00203-003-0598-4;
RA Chatterji M., Sengupta S., Nagaraja V.;
RT "Chromosomally encoded gyrase inhibitor GyrI protects Escherichia coli
RT against DNA-damaging agents.";
RL Arch. Microbiol. 180:339-346(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=11948793; DOI=10.1002/prot.10102;
RA Romanowski M.J., Gibney S.A., Burley S.K.;
RT "Crystal structure of the Escherichia coli SbmC protein that protects cells
RT from the DNA replication inhibitor microcin B17.";
RL Proteins 47:403-407(2002).
CC -!- FUNCTION: Inhibits the supercoiling activity of DNA gyrase. Acts by
CC inhibiting DNA gyrase at an early step, prior to (or at the step of)
CC binding of DNA by the gyrase. It protects cells against toxins that
CC target DNA gyrase, by inhibiting activity of these toxins and reducing
CC the formation of lethal double-strand breaks in the cell. Protects
CC cells against the natural plasmid-encoded toxins microcin B17 (MccB17)
CC and CcdB, and synthetic quinolones. Can also protect cells against
CC alkylating agents that act independently of DNA gyrase, suggesting a
CC more general role in protecting cells against DNA damage.
CC {ECO:0000269|PubMed:11850398, ECO:0000269|PubMed:13680098,
CC ECO:0000269|PubMed:8709849, ECO:0000269|PubMed:9442027}.
CC -!- SUBUNIT: Interacts with DNA gyrase. Interacts preferentially with the
CC holoenzyme composed of GyrA and GyrB, but can also weakly interact with
CC the individual GyrA and GyrB subunits. {ECO:0000269|PubMed:11777918}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By DNA-damaging agents and by the entry of cells into the
CC stationary growth phase. {ECO:0000269|PubMed:8709849}.
CC -!- SIMILARITY: Belongs to the DNA gyrase inhibitor family. {ECO:0000305}.
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DR EMBL; X84885; CAA59312.1; -; Genomic_DNA.
DR EMBL; U00009; AAA16415.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75070.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15830.1; -; Genomic_DNA.
DR PIR; H64965; H64965.
DR RefSeq; NP_416513.1; NC_000913.3.
DR RefSeq; WP_001105415.1; NZ_LN832404.1.
DR PDB; 1JYH; X-ray; 1.80 A; A=1-157.
DR PDBsum; 1JYH; -.
DR AlphaFoldDB; P33012; -.
DR SMR; P33012; -.
DR BioGRID; 4260412; 39.
DR BioGRID; 850893; 1.
DR DIP; DIP-9862N; -.
DR IntAct; P33012; 1.
DR MINT; P33012; -.
DR STRING; 511145.b2009; -.
DR jPOST; P33012; -.
DR PaxDb; P33012; -.
DR PRIDE; P33012; -.
DR EnsemblBacteria; AAC75070; AAC75070; b2009.
DR EnsemblBacteria; BAA15830; BAA15830; BAA15830.
DR GeneID; 66674095; -.
DR GeneID; 946546; -.
DR KEGG; ecj:JW1991; -.
DR KEGG; eco:b2009; -.
DR PATRIC; fig|1411691.4.peg.243; -.
DR EchoBASE; EB1838; -.
DR eggNOG; COG3449; Bacteria.
DR HOGENOM; CLU_113664_3_2_6; -.
DR InParanoid; P33012; -.
DR OMA; TPWYQFF; -.
DR PhylomeDB; P33012; -.
DR BioCyc; EcoCyc:EG11892-MON; -.
DR EvolutionaryTrace; P33012; -.
DR PRO; PR:P33012; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008657; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) inhibitor activity; IDA:CACAO.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:2000372; P:negative regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:2000104; P:negative regulation of DNA-templated DNA replication; IDA:EcoCyc.
DR Gene3D; 3.20.80.10; -; 1.
DR HAMAP; MF_01896; DNA_gyrase_inhibitor; 1.
DR InterPro; IPR010499; AraC_E-bd.
DR InterPro; IPR024911; DNA_gyrase_inhibitor_GyrI.
DR InterPro; IPR029442; GyrI-like.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR Pfam; PF06445; GyrI-like; 1.
DR SMART; SM00871; AraC_E_bind; 1.
DR SUPFAM; SSF55136; SSF55136; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Stress response.
FT CHAIN 1..157
FT /note="DNA gyrase inhibitor"
FT /id="PRO_0000083882"
FT REGION 89..96
FT /note="Required for interaction with DNA gyrase and
FT inhibition of its activity"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1JYH"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:1JYH"
FT HELIX 22..39
FT /evidence="ECO:0007829|PDB:1JYH"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1JYH"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1JYH"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1JYH"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1JYH"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1JYH"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:1JYH"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:1JYH"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1JYH"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1JYH"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1JYH"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:1JYH"
SQ SEQUENCE 157 AA; 18081 MW; C85BCD23F28C274E CRC64;
MNYEIKQEEK RTVAGFHLVG PWEQTVKKGF EQLMMWVDSK NIVPKEWVAV YYDNPDETPA
EKLRCDTVVT VPGYFTLPEN SEGVILTEIT GGQYAVAVAR VVGDDFAKPW YQFFNSLLQD
SAYEMLPKPC FEVYLNNGAE DGYWDIEMYV AVQPKHH
