Entry sw: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   02-NOV-2016, entry version 129.
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
RT   product protects cells from the DNA replication inhibitor microcin
RT   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.,
RA   Yamamoto Y., Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 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
RT   of DNA 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
RT   DNA 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
RT   cells from the DNA replication inhibitor microcin B17.";
RL   Proteins 47:403-407(2002).
CC   -!- FUNCTION: Inhibits the supercoiling activity of DNA gyrase. Acts
CC       by inhibiting DNA gyrase at an early step, prior to (or at the
CC       step of) binding of DNA by the gyrase. It protects cells against
CC       toxins that target DNA gyrase, by inhibiting activity of these
CC       toxins and reducing the formation of lethal double-strand breaks
CC       in the cell. Protects cells against the natural plasmid-encoded
CC       toxins microcin B17 (MccB17) and CcdB, and synthetic quinolones.
CC       Can also protect cells against alkylating agents that act
CC       independently of DNA gyrase, suggesting a more general role in
CC       protecting cells against DNA damage. {ECO:0000269|PubMed:11850398,
CC       ECO:0000269|PubMed:13680098, ECO:0000269|PubMed:8709849,
CC       ECO:0000269|PubMed:9442027}.
CC   -!- SUBUNIT: Interacts with DNA gyrase. Interacts preferentially with
CC       the holoenzyme composed of GyrA and GyrB, but can also weakly
CC       interact with the individual GyrA and GyrB subunits.
CC       {ECO:0000269|PubMed:11777918}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By DNA-damaging agents and by the entry of cells into
CC       the stationary growth phase. {ECO:0000269|PubMed:8709849}.
CC   -!- SIMILARITY: Belongs to the DNA gyrase inhibitor family.
CC       {ECO:0000305}.
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   ProteinModelPortal; P33012; -.
DR   SMR; P33012; -.
DR   BioGrid; 4260412; 37.
DR   DIP; DIP-9862N; -.
DR   IntAct; P33012; 1.
DR   MINT; MINT-226165; -.
DR   STRING; 511145.b2009; -.
DR   PaxDb; P33012; -.
DR   PRIDE; P33012; -.
DR   EnsemblBacteria; AAC75070; AAC75070; b2009.
DR   EnsemblBacteria; BAA15830; BAA15830; BAA15830.
DR   GeneID; 946546; -.
DR   KEGG; ecj:JW1991; -.
DR   KEGG; eco:b2009; -.
DR   PATRIC; 32119353; VBIEscCol129921_2086.
DR   EchoBASE; EB1838; -.
DR   EcoGene; EG11892; sbmC.
DR   eggNOG; ENOG4108S5C; Bacteria.
DR   eggNOG; COG3449; LUCA.
DR   HOGENOM; HOG000121896; -.
DR   InParanoid; P33012; -.
DR   KO; K07470; -.
DR   OMA; TPWYQFF; -.
DR   BioCyc; EcoCyc:EG11892-MONOMER; -.
DR   BioCyc; ECOL316407:JW1991-MONOMER; -.
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 (ATP-hydrolyzing) inhibitor activity; IDA:CACAO.
DR   GO; GO:0019899; F:enzyme binding; IPI:EcoCyc.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:2000104; P:negative regulation of DNA-dependent 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.
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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; Stress response.
FT   CHAIN         1    157       DNA gyrase inhibitor.
FT                                /FTId=PRO_0000083882.
FT   REGION       89     96       Required for interaction with DNA gyrase
FT                                and inhibition of its activity.
FT   STRAND        4      8       {ECO:0000244|PDB:1JYH}.
FT   STRAND       11     20       {ECO:0000244|PDB:1JYH}.
FT   HELIX        22     39       {ECO:0000244|PDB:1JYH}.
FT   STRAND       45     51       {ECO:0000244|PDB:1JYH}.
FT   TURN         55     57       {ECO:0000244|PDB:1JYH}.
FT   HELIX        60     62       {ECO:0000244|PDB:1JYH}.
FT   STRAND       64     71       {ECO:0000244|PDB:1JYH}.
FT   STRAND       85     89       {ECO:0000244|PDB:1JYH}.
FT   STRAND       92    101       {ECO:0000244|PDB:1JYH}.
FT   HELIX       107    117       {ECO:0000244|PDB:1JYH}.
FT   STRAND      121    125       {ECO:0000244|PDB:1JYH}.
FT   STRAND      130    134       {ECO:0000244|PDB:1JYH}.
FT   HELIX       138    141       {ECO:0000244|PDB:1JYH}.
FT   STRAND      142    154       {ECO:0000244|PDB:1JYH}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         1    155       ihamap:DNA_gyrase_inhibitor [T]
FT   MYHIT         1    153       ismart:AraC_E_bind [T]
FT   MYHIT         1    152       ipfam:GyrI-like [T]
SQ   SEQUENCE   157 AA;  18081 MW;  C85BCD23F28C274E CRC64;
     MNYEIKQEEK RTVAGFHLVG PWEQTVKKGF EQLMMWVDSK NIVPKEWVAV YYDNPDETPA
     EKLRCDTVVT VPGYFTLPEN SEGVILTEIT GGQYAVAVAR VVGDDFAKPW YQFFNSLLQD
     SAYEMLPKPC FEVYLNNGAE DGYWDIEMYV AVQPKHH
//