ID   ZAPA_YERE8              Reviewed;         109 AA.
AC   A1JPP1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=YE3398;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL13424.1; -; Genomic_DNA.
DR   RefSeq; WP_004706812.1; NC_008800.1.
DR   RefSeq; YP_001007567.1; NC_008800.1.
DR   AlphaFoldDB; A1JPP1; -.
DR   SMR; A1JPP1; -.
DR   STRING; 393305.YE3398; -.
DR   EnsemblBacteria; CAL13424; CAL13424; YE3398.
DR   GeneID; 61906681; -.
DR   GeneID; 67421525; -.
DR   KEGG; yen:YE3398; -.
DR   PATRIC; fig|393305.7.peg.3610; -.
DR   eggNOG; COG3027; Bacteria.
DR   HOGENOM; CLU_116623_3_0_6; -.
DR   OMA; NICYELH; -.
DR   PRO; PR:A1JPP1; -.
DR   Proteomes; UP000000642; 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; Septation.
FT   CHAIN           1..109
FT                   /note="Cell division protein ZapA"
FT                   /id="PRO_0000345665"
FT   COILED          22..99
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02012"
SQ   SEQUENCE   109 AA;  12655 MW;  9418EFAAA81AC057 CRC64;
     MSAQPVDIQI FGRSLRVNCP PEQQDALNMA AEDLNQRLQD LKVRTRVTNT EQLVFIAALN
     VCHELAQERL KTRDYASNME QRIRMLQQTI EQALLEQGRI SERQDAQFE