ID   DAMX_SERMA              Reviewed;         214 AA.
AC   P45459;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Cell division protein DamX {ECO:0000250|UniProtKB:P11557};
DE   Flags: Fragment;
GN   Name=damX {ECO:0000250|UniProtKB:P11557};
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sr41;
RA   Ostendorf T., Cherepanov P., Jekel M., de Vries J., Wackernagel W.;
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Non-essential cell division protein.
CC       {ECO:0000250|UniProtKB:P11557}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P11557}; Single-pass membrane protein
CC       {ECO:0000255}. Note=Localizes at the septal ring.
CC       {ECO:0000250|UniProtKB:P11557}.
CC   -!- DOMAIN: The SPOR domain binds septal peptidoglycans and is required to
CC       target DamX to the septal ring. {ECO:0000250|UniProtKB:P11557}.
CC   -!- SIMILARITY: Belongs to the DamX family. {ECO:0000305}.
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DR   EMBL; X78412; CAA55176.1; -; Genomic_DNA.
DR   PIR; S47098; S47098.
DR   AlphaFoldDB; P45459; -.
DR   SMR; P45459; -.
DR   STRING; 273526.SMDB11_3849; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.1070; -; 1.
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   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..214
FT                   /note="Cell division protein DamX"
FT                   /id="PRO_0000079780"
FT   TRANSMEM        44..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          127..204
FT                   /note="SPOR"
FT                   /evidence="ECO:0000305"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   214 AA;  22157 MW;  3D1BDD43F8D6C401 CRC64;
     GSGTPTEAQT QPQQGGAHER VDLPGNMADA LSQQQGQVDA ATQGMTGAAS TLPTAPATVM
     SGAAAREATR PVQGTAPQQH KTPAKTAAAK PTATQHKSPT TVYTPPAKPS STAKAGAVAS
     SGSSVQSAPG SHYTLQLSSA SRSDTLNAYA KQQKLQNYLV YATKRDGKPW YVLVSGNYAS
     SAEAKRAIAS LPADVQAKKP WVRPVHQVQQ DLKK