ID   ZAPA_SALPA              Reviewed;         109 AA.
AC   Q5PJH4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=SPA2928;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78769.1; -; Genomic_DNA.
DR   RefSeq; WP_001276011.1; NC_006511.1.
DR   AlphaFoldDB; Q5PJH4; -.
DR   SMR; Q5PJH4; -.
DR   EnsemblBacteria; AAV78769; AAV78769; SPA2928.
DR   GeneID; 66757358; -.
DR   KEGG; spt:SPA2928; -.
DR   HOGENOM; CLU_116623_3_0_6; -.
DR   OMA; NICYELH; -.
DR   Proteomes; UP000008185; 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_0000345655"
FT   COILED          21..97
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02012"
SQ   SEQUENCE   109 AA;  12523 MW;  2677651A6E9F8C98 CRC64;
     MSAQPVDIQI FGRSLRVNCP PDQRDALNQA ADDLNQRLQD LKVRTRVTNT EQLVFIAALN
     ISYELTQEKA KTRDYAASME QRIRMLQQTI EQALLDQGRI TEKTGQNFE