ZAPA_ECO45
ID ZAPA_ECO45 Reviewed; 109 AA.
AC B7MM96;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=ECS88_3190;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928161; CAR04425.1; -; Genomic_DNA.
DR RefSeq; WP_001276008.1; NC_011742.1.
DR AlphaFoldDB; B7MM96; -.
DR SMR; B7MM96; -.
DR EnsemblBacteria; CAR04425; CAR04425; ECS88_3190.
DR GeneID; 67415204; -.
DR KEGG; ecz:ECS88_3190; -.
DR HOGENOM; CLU_116623_3_0_6; -.
DR OMA; NICYELH; -.
DR Proteomes; UP000000747; 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_1000189507"
FT COILED 21..99
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02012"
SQ SEQUENCE 109 AA; 12594 MW; 26777CC2B2B71148 CRC64;
MSAQPVDIQI FGRSLRVNCP PDQRDALNQA ADDLNQRLQD LKERTRVTNT EQLVFIAALN
ISYELAQEKA KTRDYAASME QRIRMLQQTI EQALLEQGRI TEKTNQNFE