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ZAPA_SHIDS
ID   ZAPA_SHIDS              Reviewed;         109 AA.
AC   Q32BX2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Cell division protein ZapA {ECO:0000255|HAMAP-Rule:MF_02012};
DE   AltName: Full=Z ring-associated protein ZapA {ECO:0000255|HAMAP-Rule:MF_02012};
GN   Name=zapA {ECO:0000255|HAMAP-Rule:MF_02012}; OrderedLocusNames=SDY_3171;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Activator of cell division through the inhibition of FtsZ
CC       GTPase activity, therefore promoting FtsZ assembly into bundles of
CC       protofilaments necessary for the formation of the division Z ring. It
CC       is recruited early at mid-cell but it is not essential for cell
CC       division. {ECO:0000255|HAMAP-Rule:MF_02012}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_02012}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02012}.
CC       Note=Localizes at mid-cell. {ECO:0000255|HAMAP-Rule:MF_02012}.
CC   -!- SIMILARITY: Belongs to the ZapA family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02012}.
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DR   EMBL; CP000034; ABB63183.1; -; Genomic_DNA.
DR   RefSeq; WP_001276009.1; NC_007606.1.
DR   RefSeq; YP_404674.1; NC_007606.1.
DR   AlphaFoldDB; Q32BX2; -.
DR   SMR; Q32BX2; -.
DR   STRING; 300267.SDY_3171; -.
DR   EnsemblBacteria; ABB63183; ABB63183; SDY_3171.
DR   KEGG; sdy:SDY_3171; -.
DR   PATRIC; fig|300267.13.peg.3789; -.
DR   HOGENOM; CLU_116623_3_0_6; -.
DR   OMA; NICYELH; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.880; -; 1.
DR   HAMAP; MF_02012; ZapA_type1; 1.
DR   InterPro; IPR007838; Cell_div_ZapA-like.
DR   InterPro; IPR036192; Cell_div_ZapA-like_sf.
DR   InterPro; IPR023771; Cell_div_ZapA_eubact.
DR   InterPro; IPR042233; Cell_div_ZapA_N.
DR   PANTHER; PTHR34981; PTHR34981; 1.
DR   Pfam; PF05164; ZapA; 1.
DR   SUPFAM; SSF102829; SSF102829; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Reference proteome;
KW   Septation.
FT   CHAIN           1..109
FT                   /note="Cell division protein ZapA"
FT                   /id="PRO_0000345661"
FT   COILED          21..100
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02012"
SQ   SEQUENCE   109 AA;  12622 MW;  26777CC2B1781148 CRC64;
     MSAQPVDIQI FGRSLRVNCP PDQRDALNQA ADDLNQRLQD LKERTRVTNT EQLVFIAALN
     ISYELAQEKA KTRDYAASME QRIRMLQQTI EQALLERGRI TEKTNQNFE
 
 
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