ID   BOLA_ECOLI              Reviewed;         105 AA.
AC   P0ABE2; P15298; Q2MBZ1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=DNA-binding transcriptional regulator BolA {ECO:0000305};
GN   Name=bolA {ECO:0000303|PubMed:305364}; OrderedLocusNames=b0435, JW5060;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=2684651; DOI=10.1002/j.1460-2075.1989.tb08573.x;
RA   Aldea M., Garrido T., Hernandez-Chico C., Vicente M., Kushner S.R.;
RT   "Induction of a growth-phase-dependent promoter triggers transcription of
RT   bolA, an Escherichia coli morphogene.";
RL   EMBO J. 8:3923-3931(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX   PubMed=8231804; DOI=10.1111/j.1365-2958.1993.tb01731.x;
RA   Lindquist S., Weston-Hafer K., Schmidt H., Pul C., Korfmann G.,
RA   Erickson J., Sanders C., Martin H.H., Normark S.;
RT   "AmpG, a signal transducer in chromosomal beta-lactamase induction.";
RL   Mol. Microbiol. 9:703-715(1993).
RN   [6]
RP   FUNCTION IN MORPHOGENETIC PATHWAY.
RX   PubMed=305364;
RA   Aldea M., Hernandez-Chico C., de la Campa A.G., Kushner S.R., Vicente M.;
RT   "Identification, cloning, and expression of bolA, an ftsZ-dependent
RT   morphogene of Escherichia coli.";
RL   J. Bacteriol. 170:5169-5176(1988).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=10361282; DOI=10.1046/j.1365-2958.1999.01397.x;
RA   Santos J.M., Freire P., Vicente M., Arraiano C.M.;
RT   "The stationary-phase morphogene bolA from Escherichia coli is induced by
RT   stress during early stages of growth.";
RL   Mol. Microbiol. 32:789-798(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=12354237; DOI=10.1046/j.1365-2958.2002.03131.x;
RA   Santos J.M., Lobo M., Matos A.P., De Pedro M.A., Arraiano C.M.;
RT   "The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC),
RT   promoting normal morphology in Escherichia coli.";
RL   Mol. Microbiol. 45:1729-1740(2002).
RN   [9]
RP   FUNCTION IN BIOFILM DEVELOPMENT.
RX   PubMed=15345459; DOI=10.1128/aem.70.9.5682-5684.2004;
RA   Vieira H.L., Freire P., Arraiano C.M.;
RT   "Effect of Escherichia coli morphogene bolA on biofilms.";
RL   Appl. Environ. Microbiol. 70:5682-5684(2004).
RN   [10]
RP   FUNCTION PREDICTION.
RX   PubMed=15670813; DOI=10.1016/j.febslet.2004.11.111;
RA   Huynen M.A., Spronk C.A., Gabaldon T., Snel B.;
RT   "Combining data from genomes, Y2H and 3D structure indicates that BolA is a
RT   reductase interacting with a glutaredoxin.";
RL   FEBS Lett. 579:591-596(2005).
RN   [11]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=19111750; DOI=10.1016/j.jmb.2008.12.026;
RA   Freire P., Moreira R.N., Arraiano C.M.;
RT   "BolA inhibits cell elongation and regulates MreB expression levels.";
RL   J. Mol. Biol. 385:1345-1351(2009).
RN   [12]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=21464593;
RA   Guinote I.B., Matos R.G., Freire P., Arraiano C.M.;
RT   "BolA affects cell growth, and binds to the promoters of penicillin-binding
RT   proteins 5 and 6 and regulates their expression.";
RL   J. Microbiol. Biotechnol. 21:243-251(2011).
RN   [13]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=25691594; DOI=10.1128/mbio.02352-14;
RA   Dressaire C., Moreira R.N., Barahona S., Alves de Matos A.P.,
RA   Arraiano C.M.;
RT   "BolA is a transcriptional switch that turns off motility and turns on
RT   biofilm development.";
RL   MBio 6:E02352-E02352(2015).
RN   [14]
RP   STRUCTURE BY NMR OF 1-100.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the bolA protein from Escherichia coli.";
RL   Submitted (SEP-2006) to the PDB data bank.
CC   -!- FUNCTION: Transcriptional regulator that plays an important role in
CC       general stress response. Has many effects on cell morphology, cell
CC       growth and cell division. Acts by regulating the transcription of many
CC       genes, including dacA (PBP-5), dacC (PBP-6), ampC and mreB. Probably
CC       involved in the coordination of genes that adapt the cell physiology in
CC       order to enhance cell adaptation and survival under stress conditions.
CC       Essential for normal cell morphology in stationary phase and under
CC       conditions of starvation (PubMed:10361282, PubMed:12354237,
CC       PubMed:19111750, PubMed:21464593, PubMed:25691594). Also regulates a
CC       complex network of genes encoding proteins related to biofilm
CC       development, and negatively modulates flagellar biosynthesis and
CC       swimming capacity. Could be a motile/adhesive transcriptional switch,
CC       specifically involved in the transition between the planktonic and the
CC       attachment stage of biofilm formation (PubMed:25691594). Overexpression
CC       produces round cell shape, impairs cell growth rate and induces biofilm
CC       development (PubMed:305364, PubMed:15345459, PubMed:21464593).
CC       {ECO:0000269|PubMed:10361282, ECO:0000269|PubMed:12354237,
CC       ECO:0000269|PubMed:15345459, ECO:0000269|PubMed:19111750,
CC       ECO:0000269|PubMed:21464593, ECO:0000269|PubMed:25691594,
CC       ECO:0000269|PubMed:305364}.
CC   -!- INTERACTION:
CC       P0ABE2; P0AC69: grxD; NbExp=5; IntAct=EBI-545774, EBI-545828;
CC       P0ABE2; P33361: yehY; NbExp=3; IntAct=EBI-545774, EBI-545876;
CC   -!- INDUCTION: Induced during the transition to the stationary phase, under
CC       the control of the sigma factor RpoS (PubMed:2684651). Also induced
CC       during early logarithmic growth in response to several forms of stress
CC       (heat shock, acidic stress, oxidative stress, carbon-starvation stress
CC       and osmotic shock), and this induction can be partially RpoS
CC       independent (PubMed:10361282). {ECO:0000269|PubMed:10361282,
CC       ECO:0000269|PubMed:2684651}.
CC   -!- MISCELLANEOUS: Was predicted, by combining genome sequences, physical
CC       interactions and 3D structures analyses, to be a reductase that
CC       interacts with a glutaredoxin. {ECO:0000305|PubMed:15670813}.
CC   -!- SIMILARITY: Belongs to the BolA/IbaG family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB28882.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAB40191.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA35633.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X17642; CAA35633.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U82664; AAB40191.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73538.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76215.1; -; Genomic_DNA.
DR   EMBL; S67816; AAB28882.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_414969.4; NC_000913.3.
DR   RefSeq; WP_000973448.1; NZ_STEB01000007.1.
DR   PDB; 2DHM; NMR; -; A=1-100.
DR   PDBsum; 2DHM; -.
DR   AlphaFoldDB; P0ABE2; -.
DR   SMR; P0ABE2; -.
DR   BioGRID; 4259840; 529.
DR   BioGRID; 851382; 10.
DR   ComplexPortal; CPX-5898; bolA-grxD iron-sulfur cluster assembly complex.
DR   DIP; DIP-47926N; -.
DR   IntAct; P0ABE2; 13.
DR   STRING; 511145.b0435; -.
DR   jPOST; P0ABE2; -.
DR   PaxDb; P0ABE2; -.
DR   PRIDE; P0ABE2; -.
DR   EnsemblBacteria; AAC73538; AAC73538; b0435.
DR   EnsemblBacteria; BAE76215; BAE76215; BAE76215.
DR   GeneID; 66671263; -.
DR   GeneID; 947043; -.
DR   KEGG; ecj:JW5060; -.
DR   KEGG; eco:b0435; -.
DR   PATRIC; fig|511145.12.peg.452; -.
DR   EchoBASE; EB0123; -.
DR   eggNOG; COG0271; Bacteria.
DR   HOGENOM; CLU_109462_3_1_6; -.
DR   InParanoid; P0ABE2; -.
DR   OMA; CLGGFGK; -.
DR   PhylomeDB; P0ABE2; -.
DR   BioCyc; EcoCyc:EG10125-MON; -.
DR   EvolutionaryTrace; P0ABE2; -.
DR   PRO; PR:P0ABE2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:1990229; C:iron-sulfur cluster assembly complex; IPI:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IC:ComplexPortal.
DR   GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEP:EcoCyc.
DR   Gene3D; 3.30.300.90; -; 1.
DR   InterPro; IPR002634; BolA.
DR   InterPro; IPR036065; BolA-like_sf.
DR   Pfam; PF01722; BolA; 1.
DR   PIRSF; PIRSF003113; BolA; 1.
DR   SUPFAM; SSF82657; SSF82657; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW   Stress response; Transcription; Transcription regulation.
FT   CHAIN           1..105
FT                   /note="DNA-binding transcriptional regulator BolA"
FT                   /id="PRO_0000201212"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:2DHM"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:2DHM"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:2DHM"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:2DHM"
FT   HELIX           55..63
FT                   /evidence="ECO:0007829|PDB:2DHM"
FT   HELIX           65..69
FT                   /evidence="ECO:0007829|PDB:2DHM"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:2DHM"
FT   HELIX           82..86
FT                   /evidence="ECO:0007829|PDB:2DHM"
SQ   SEQUENCE   105 AA;  11994 MW;  7499BFB6228E66F3 CRC64;
     MMIRERIEEK LRAAFQPVFL EVVDESYRHN VPAGSESHFK VVLVSDRFTG ERFLNRHRMI
     YSTLAEELST TVHALALHTY TIKEWEGLQD TVFASPPCRG AGSIA