ZAPA_SALTI
ID ZAPA_SALTI Reviewed; 109 AA.
AC Q8XGR5; Q7AMB9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 105.
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};
GN OrderedLocusNames=STY3216, t2978;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
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; AE014613; AAO70530.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD02890.1; -; Genomic_DNA.
DR RefSeq; NP_457458.1; NC_003198.1.
DR RefSeq; WP_001276011.1; NZ_WSUR01000024.1.
DR AlphaFoldDB; Q8XGR5; -.
DR SMR; Q8XGR5; -.
DR STRING; 220341.16504143; -.
DR EnsemblBacteria; AAO70530; AAO70530; t2978.
DR GeneID; 66757358; -.
DR KEGG; stt:t2978; -.
DR KEGG; sty:STY3216; -.
DR PATRIC; fig|220341.7.peg.3277; -.
DR eggNOG; COG3027; Bacteria.
DR HOGENOM; CLU_116623_3_0_6; -.
DR OMA; NICYELH; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000345657"
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