ID D8MUY1_ERWBE Unreviewed; 238 AA.
AC D8MUY1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Cell division protein DedD {ECO:0000256|HAMAP-Rule:MF_02022};
GN Name=dedD {ECO:0000256|HAMAP-Rule:MF_02022};
GN OrderedLocusNames=EbC_31070 {ECO:0000313|EMBL:CAX60638.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX60638.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60638.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- FUNCTION: Non-essential cell division protein that could be required
CC for efficient cell constriction. {ECO:0000256|HAMAP-Rule:MF_02022}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02022}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02022}. Note=Localizes at the septal ring. {ECO:0000256|HAMAP-
CC Rule:MF_02022}.
CC -!- DOMAIN: The SPOR domain binds septal peptidoglycans and is required to
CC target DedD to the septal ring. {ECO:0000256|HAMAP-Rule:MF_02022}.
CC -!- SIMILARITY: Belongs to the DedD family. {ECO:0000256|HAMAP-
CC Rule:MF_02022}.
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DR EMBL; FP236843; CAX60638.1; -; Genomic_DNA.
DR RefSeq; WP_013203123.1; NC_014306.1.
DR AlphaFoldDB; D8MUY1; -.
DR STRING; 634500.EbC_31070; -.
DR KEGG; ebi:EbC_31070; -.
DR eggNOG; COG3147; Bacteria.
DR HOGENOM; CLU_068683_1_1_6; -.
DR Proteomes; UP000008793; Chromosome.
DR GO; GO:0030428; C:cell septum; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0032506; P:cytokinetic process; IEA:InterPro.
DR Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR HAMAP; MF_02022; DedD; 1.
DR InterPro; IPR032898; DedD.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
DR PANTHER; PTHR38687:SF1; CELL DIVISION PROTEIN DEDD; 1.
DR PANTHER; PTHR38687; CELL DIVISION PROTEIN DEDD-RELATED; 1.
DR Pfam; PF05036; SPOR; 1.
DR SUPFAM; SSF110997; Sporulation related repeat; 1.
DR PROSITE; PS51724; SPOR; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02022};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02022};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02022};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02022};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_02022};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02022};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02022}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02022"
FT DOMAIN 156..235
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 44..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 24923 MW; 4B21C138DC671382 CRC64;
MASKFQNRLV GTVIIVALGV IILPGLLDGK KKHYKEEFAA IPLVPKPGDQ QENDLVPPVT
QSLPSQPPEG AATAVEGKTP GNTSQAESGS TAPKSANKPS VISPPPMVES KPVQQPKPVE
KPKPKPVEKT VEKPKAQPKA EPKPEPAPQA AEPESAPTGQ AYVVQLGALK NASKVNQVVA
QLRLSGYRAF TVPSTPVQGE ITRIYVGPDA SKAKMQASIS ELKGISGLGG VVKPYSAR
//
