DRPB_ECOLI
ID DRPB_ECOLI Reviewed; 100 AA.
AC P76334; Q2MAZ9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cell division protein DrpB {ECO:0000255|HAMAP-Rule:MF_00857, ECO:0000303|PubMed:32900831};
DE AltName: Full=Division ring protein B {ECO:0000255|HAMAP-Rule:MF_00857, ECO:0000303|PubMed:32900831};
GN Name=drpB {ECO:0000255|HAMAP-Rule:MF_00857, ECO:0000303|PubMed:32900831};
GN Synonyms=yedR; OrderedLocusNames=b1963, JW1946;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [4]
RP FUNCTION, SEQUENCE REVISION TO N-TERMINUS, SUBUNIT, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=32900831; DOI=10.1128/jb.00284-20;
RA Yahashiri A., Babor J.T., Anwar A.L., Bezy R.P., Piette E.W.,
RA Ryan Arends S.J., Mueh U., Steffen M.R., Cline J.M., Stanek D.N.,
RA Lister S.D., Swanson S.M., Weiss D.S.;
RT "DrpB (YedR) is a non-essential cell division protein in Escherichia
RT coli.";
RL J. Bacteriol. 0:0-0(2020).
CC -!- FUNCTION: A non-essential division protein that localizes to the septal
CC ring in low ionic strength medium. {ECO:0000255|HAMAP-Rule:MF_00857}.
CC -!- FUNCTION: Localizes to the septal ring in about 30% of observed cells
CC before cell constriction occurs; localization occurs in low ionic
CC strength medium (0 NaCl) and requires FtsZ but not FtsEX.
CC Overexpression partially restores correct FtsI localization to the
CC division septum in an ftsEX deletion. Isolated as a multicopy
CC suppressor of an ftsEX deletion mutant; it does not suppress other cell
CC division defects (e.g. ftsA, ftsI, ftsQ or ftsZ).
CC {ECO:0000269|PubMed:32900831}.
CC -!- SUBUNIT: Bacterial adenylate cyclase hybrid (BACTH) studies show
CC interaction of this protein with DamX, FtsI, FtsN, FtsQ, YmgF, DedD,
CC FtsA and MalF, as well as weaker interactions with DedD, MalG and PBP2,
CC but this assay often generates false positive results.
CC {ECO:0000269|PubMed:32900831}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00857, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00857, ECO:0000305|PubMed:15919996}.
CC Note=Localizes to the septal ring before constriction, only when cells
CC are grown at low ionic strength. {ECO:0000255|HAMAP-Rule:MF_00857,
CC ECO:0000269|PubMed:32900831}.
CC -!- INDUCTION: Constitutively expressed at low levels in mid log phase, in
CC high (10 g/ml NaCl) and low (0 g/ml NaCl) ionic strength medium (at
CC protein level). {ECO:0000269|PubMed:32900831}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in rich, rich without NaCl
CC or minimal medium. Double dedD-drpB deletion mutants grow 1000-fold
CC less well at 42 degrees Celsius and are filamentous when grown on LB,
CC no effect is seen in low ionic strength medium; few septa are observed.
CC {ECO:0000269|PubMed:32900831}.
CC -!- SIMILARITY: Belongs to the DrpB family. {ECO:0000255|HAMAP-
CC Rule:MF_00857}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC75029.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000269|PubMed:32900831};
CC Sequence=BAE76557.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000269|PubMed:32900831};
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DR EMBL; U00096; AAC75029.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP009048; BAE76557.1; ALT_INIT; Genomic_DNA.
DR PIR; G64960; G64960.
DR RefSeq; NP_416472.2; NC_000913.3.
DR RefSeq; WP_001313057.1; NZ_STEB01000050.1.
DR AlphaFoldDB; P76334; -.
DR BioGRID; 4260864; 148.
DR BioGRID; 850828; 1.
DR DIP; DIP-11849N; -.
DR IntAct; P76334; 1.
DR STRING; 511145.b1963; -.
DR PaxDb; P76334; -.
DR PRIDE; P76334; -.
DR DNASU; 946477; -.
DR EnsemblBacteria; AAC75029; AAC75029; b1963.
DR EnsemblBacteria; BAE76557; BAE76557; BAE76557.
DR GeneID; 946477; -.
DR KEGG; ecj:JW1946; -.
DR KEGG; eco:b1963; -.
DR PATRIC; fig|511145.12.peg.2042; -.
DR EchoBASE; EB3795; -.
DR eggNOG; ENOG5032VGN; Bacteria.
DR HOGENOM; CLU_168880_1_0_6; -.
DR PhylomeDB; P76334; -.
DR BioCyc; EcoCyc:G7051-MON; -.
DR PRO; PR:P76334; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR HAMAP; MF_00857; DrpB; 1.
DR InterPro; IPR046385; DrpB.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..100
FT /note="Cell division protein DrpB"
FT /id="PRO_0000169101"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00857"
FT TOPO_DOM 38..64
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00857"
FT TOPO_DOM 86..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 100 AA; 11325 MW; 2776DB1BEBB94D75 CRC64;
MEYGSTKMEE RLSRSPGGKL ALWAFYTWCG YFVWAMARYI WVMSRIPDAP VSGFESDLGS
TAGKWLGALV GFLFMALVGA LLGSIAWYTR PRPARSRRYE
