ID A0A085U4Y8_YERRU Unreviewed; 241 AA.
AC A0A085U4Y8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Cell division protein DedD {ECO:0000256|HAMAP-Rule:MF_02022};
GN Name=dedD {ECO:0000256|HAMAP-Rule:MF_02022};
GN ORFNames=CSF007_12530 {ECO:0000313|EMBL:CEK28245.1}, NCTC10476_03211
GN {ECO:0000313|EMBL:SUQ01828.1};
OS Yersinia ruckeri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=29486 {ECO:0000313|EMBL:CEK28245.1};
RN [1] {ECO:0000313|EMBL:CEK28245.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CSF007-82 {ECO:0000313|EMBL:CEK28245.1};
RA Nelson M.C., LaPatra S.E., Welch T.J., Graf J.;
RT "Complete Genome Sequence of Yersinia ruckeri Strain CSF007-82, Etiologic
RT Agent of Red Mouth Disease in Salmonid Fish.";
RL Genome Announc. 3:1-2(2015).
RN [2] {ECO:0000313|EMBL:SUQ01828.1, ECO:0000313|Proteomes:UP000255169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10476 {ECO:0000313|EMBL:SUQ01828.1,
RC ECO:0000313|Proteomes:UP000255169};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; LN681231; CEK28245.1; -; Genomic_DNA.
DR EMBL; UHJG01000001; SUQ01828.1; -; Genomic_DNA.
DR RefSeq; WP_038244265.1; NZ_VDHI01000003.1.
DR AlphaFoldDB; A0A085U4Y8; -.
DR STRING; 29486.UGYR_04935; -.
DR GeneID; 66880137; -.
DR KEGG; yrb:UGYR_04935; -.
DR PATRIC; fig|29486.44.peg.2673; -.
DR eggNOG; COG3147; Bacteria.
DR OrthoDB; 7069135at2; -.
DR Proteomes; UP000255169; Unassembled WGS sequence.
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:UP000255169};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02022};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02022}.
FT TRANSMEM 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02022"
FT DOMAIN 158..237
FT /note="SPOR"
FT /evidence="ECO:0000259|PROSITE:PS51724"
FT REGION 60..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 25381 MW; A7210F69EC99A8B2 CRC64;
MASKFQNRLV GTVILVALGV ILLPGLLDGK KKHYEDEFAA IPLVPKPGDA EEIDVVPPVN
QPLPMQPPEG AAEALSATKG AEPVSPAANE AGNLSAQPTL VAPPPVEIKP VESRPVEKKP
VVPKPVEVKP KVEVKPVEVK PKPEVKPVEV KPSSEEKTPA GQAYVVQLGA LKNAAKVDEV
VAKLRLSGHR AYTVPSTPVQ GQITRIYVGP DASKQNLQSA LPELNALSGL TGQVKAYSTG
R
//
