DEDD_ECOLI
ID DEDD_ECOLI Reviewed; 220 AA.
AC P09549;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cell division protein DedD {ECO:0000255|HAMAP-Rule:MF_02022, ECO:0000305};
GN Name=dedD {ECO:0000255|HAMAP-Rule:MF_02022, ECO:0000303|PubMed:3040734};
GN OrderedLocusNames=b2314, JW5378;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3040734; DOI=10.1016/s0021-9258(18)45338-0;
RA Nonet M.L., Marvel C.C., Tolan D.R.;
RT "The hisT-purF region of the Escherichia coli K-12 chromosome.
RT Identification of additional genes of the hisT and purF operons.";
RL J. Biol. Chem. 262:12209-12217(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19684127; DOI=10.1128/jb.00811-09;
RA Gerding M.A., Liu B., Bendezu F.O., Hale C.A., Bernhardt T.G.,
RA de Boer P.A.;
RT "Self-enhanced accumulation of FtsN at division sites and roles for other
RT proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell
RT constriction.";
RL J. Bacteriol. 191:7383-7401(2009).
RN [6]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=K12 / BW25113;
RX PubMed=19880599; DOI=10.1128/jb.01244-09;
RA Arends S.J., Williams K., Scott R.J., Rolong S., Popham D.L., Weiss D.S.;
RT "Discovery and characterization of three new Escherichia coli septal ring
RT proteins that contain a SPOR domain: DamX, DedD, and RlpA.";
RL J. Bacteriol. 192:242-255(2010).
RN [7]
RP 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: Non-essential cell division protein that could be required
CC for efficient cell constriction. {ECO:0000255|HAMAP-Rule:MF_02022,
CC ECO:0000269|PubMed:19684127}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02022, ECO:0000305}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02022}. Note=Localizes at the septal ring.
CC {ECO:0000255|HAMAP-Rule:MF_02022, ECO:0000269|PubMed:19684127,
CC ECO:0000269|PubMed:19880599}.
CC -!- DOMAIN: The SPOR domain binds septal peptidoglycans and is required to
CC target DedD to the septal ring. {ECO:0000255|HAMAP-Rule:MF_02022,
CC ECO:0000269|PubMed:19880599}.
CC -!- DISRUPTION PHENOTYPE: Deletion causes a mild cell chaining phenotype
CC (PubMed:19684127). 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 osmolarity medium; few septa are observed
CC (PubMed:32900831). {ECO:0000269|PubMed:19684127,
CC ECO:0000269|PubMed:32900831}.
CC -!- SIMILARITY: Belongs to the DedD family. {ECO:0000255|HAMAP-
CC Rule:MF_02022, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23967.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M68934; AAA23967.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75374.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16162.2; -; Genomic_DNA.
DR PIR; H65003; XMECDD.
DR RefSeq; NP_416817.2; NC_000913.3.
DR RefSeq; WP_000146992.1; NZ_STEB01000008.1.
DR PDB; 6ZTG; NMR; -; A=28-220.
DR PDBsum; 6ZTG; -.
DR AlphaFoldDB; P09549; -.
DR SMR; P09549; -.
DR BioGRID; 4260528; 50.
DR STRING; 511145.b2314; -.
DR jPOST; P09549; -.
DR PaxDb; P09549; -.
DR PRIDE; P09549; -.
DR EnsemblBacteria; AAC75374; AAC75374; b2314.
DR EnsemblBacteria; BAA16162; BAA16162; BAA16162.
DR GeneID; 58388066; -.
DR GeneID; 944971; -.
DR KEGG; ecj:JW5378; -.
DR KEGG; eco:b2314; -.
DR PATRIC; fig|511145.12.peg.2409; -.
DR EchoBASE; EB0214; -.
DR eggNOG; COG3147; Bacteria.
DR HOGENOM; CLU_068683_1_1_6; -.
DR OMA; GYNAYIR; -.
DR PhylomeDB; P09549; -.
DR BioCyc; EcoCyc:EG10218-MON; -.
DR PRO; PR:P09549; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0030428; C:cell septum; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008047; F:enzyme activator activity; IDA:EcoCyc.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:EcoCyc.
DR GO; GO:0032506; P:cytokinetic process; IMP:EcoCyc.
DR Gene3D; 3.30.70.1070; -; 1.
DR HAMAP; MF_02022; DedD; 1.
DR InterPro; IPR032898; DedD.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
DR Pfam; PF05036; SPOR; 1.
DR SUPFAM; SSF110997; SSF110997; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..220
FT /note="Cell division protein DedD"
FT /id="PRO_0000079851"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02022"
FT DOMAIN 138..217
FT /note="SPOR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02022"
FT REGION 46..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6ZTG"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6ZTG"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 139..152
FT /evidence="ECO:0007829|PDB:6ZTG"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:6ZTG"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:6ZTG"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:6ZTG"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:6ZTG"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6ZTG"
SQ SEQUENCE 220 AA; 22938 MW; 454529DCB8AC1644 CRC64;
MASKFQNRLV GTIVLVALGV IVLPGLLDGQ KKHYQDEFAA IPLVPKAGDR DEPDMMPAAT
QALPTQPPEG AAEEVRAGDA AAPSLDPATI AANNTEFEPE PAPVAPPKPK PVEPPKPKVE
APPAPKPEPK PVVEEKAAPT GKAYVVQLGA LKNADKVNEI VGKLRGAGYR VYTSPSTPVQ
GKITRILVGP DASKDKLKGS LGELKQLSGL SGVVMGYTPN
