ZAPA_SALPC
ID ZAPA_SALPC Reviewed; 109 AA.
AC C0PY34;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=SPC_3121;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000857; ACN47208.1; -; Genomic_DNA.
DR RefSeq; WP_001276011.1; NC_012125.1.
DR AlphaFoldDB; C0PY34; -.
DR SMR; C0PY34; -.
DR EnsemblBacteria; ACN47208; ACN47208; SPC_3121.
DR GeneID; 66757358; -.
DR KEGG; sei:SPC_3121; -.
DR HOGENOM; CLU_116623_3_0_6; -.
DR OMA; NICYELH; -.
DR Proteomes; UP000001599; 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_1000189523"
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