ID   DAMX_ECO57              Reviewed;         428 AA.
AC   Q8X826;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cell division protein DamX {ECO:0000255|HAMAP-Rule:MF_02021};
GN   Name=damX {ECO:0000255|HAMAP-Rule:MF_02021};
GN   OrderedLocusNames=Z4741, ECs4230;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Non-essential cell division protein. {ECO:0000255|HAMAP-
CC       Rule:MF_02021}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02021}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02021}. Note=Localizes at the septal ring. {ECO:0000255|HAMAP-
CC       Rule:MF_02021}.
CC   -!- DOMAIN: The SPOR domain binds septal peptidoglycans and is required to
CC       target DamX to the septal ring. {ECO:0000255|HAMAP-Rule:MF_02021}.
CC   -!- SIMILARITY: Belongs to the DamX family. {ECO:0000255|HAMAP-
CC       Rule:MF_02021}.
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DR   EMBL; AE005174; AAG58488.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37653.1; -; Genomic_DNA.
DR   PIR; D86003; D86003.
DR   PIR; F91157; F91157.
DR   RefSeq; NP_312257.1; NC_002695.1.
DR   RefSeq; WP_000343210.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X826; -.
DR   BMRB; Q8X826; -.
DR   SMR; Q8X826; -.
DR   STRING; 155864.EDL933_4586; -.
DR   EnsemblBacteria; AAG58488; AAG58488; Z4741.
DR   EnsemblBacteria; BAB37653; BAB37653; ECs_4230.
DR   GeneID; 915914; -.
DR   KEGG; ece:Z4741; -.
DR   KEGG; ecs:ECs_4230; -.
DR   PATRIC; fig|386585.9.peg.4416; -.
DR   eggNOG; COG3266; Bacteria.
DR   HOGENOM; CLU_048276_1_0_6; -.
DR   OMA; ASRQYIM; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0030428; C:cell septum; IEA:InterPro.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0032506; P:cytokinetic process; IEA:InterPro.
DR   Gene3D; 3.30.70.1070; -; 1.
DR   HAMAP; MF_02021; DamX; 1.
DR   InterPro; IPR032899; DamX.
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; Coiled coil;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..428
FT                   /note="Cell division protein DamX"
FT                   /id="PRO_0000079778"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02021"
FT   DOMAIN          342..419
FT                   /note="SPOR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02021"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          55..87
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02021"
FT   COMPBIAS        1..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..79
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  46104 MW;  50D4A9527951058E CRC64;
     MDEFKPEDEL KPDPSDRRTG RSRQSSERSE RTERGEPQIN FDDIELDDTD DRRPTRAQKE
     RNEEPEIEEE IDESEDETVD EERVERRPRK RKKAASKPAS RQYMMMGVGI LVLLLLIIGI
     GSALKAPSTT SSDQTASGEK SIDLAGNATD QANGVQPAPG TTSAENTQQD VSLPPISSTP
     TQGQTPAATD GQQRVEVQGD LNNALTQPQN QQQLNNVAVN STLPTEPATV APVRNGNASR
     DTAKTQTAER PATTRPARQQ AVIEPKKPQA TVKTEPKPVA QTPKRTEPAA PVASTKAPAA
     TSTPAPKETA TTAPVQTASP AQTTATPAAG GKTAGNVGSL KSAPSSHYTL QLSSSSNYDN
     LNGWAKKENL KNYVVYETTR NGQPWYVLVS GVYASKEEAK KAVSTLPADV QAKNPWAKPL
     RQVQADLK