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Database: UniProt
Entry: ZAPA_YERPS
LinkDB: ZAPA_YERPS
Original site: ZAPA_YERPS 
ID   ZAPA_YERPS              Reviewed;         109 AA.
AC   Q666R0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=YPTB3187;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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; BX936398; CAH22425.1; -; Genomic_DNA.
DR   RefSeq; WP_002209954.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q666R0; -.
DR   SMR; Q666R0; -.
DR   GeneID; 66844382; -.
DR   KEGG; ypo:BZ17_3424; -.
DR   KEGG; yps:YPTB3187; -.
DR   PATRIC; fig|273123.14.peg.3593; -.
DR   Proteomes; UP000001011; 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; 1.20.5.50; -; 1.
DR   Gene3D; 3.30.160.880; Cell division protein ZapA protomer, N-terminal domain; 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; CELL DIVISION PROTEIN ZAPA; 1.
DR   PANTHER; PTHR34981:SF1; CELL DIVISION PROTEIN ZAPA; 1.
DR   Pfam; PF05164; ZapA; 1.
DR   SUPFAM; SSF102829; Cell division protein ZapA-like; 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_0000345670"
FT   COILED          22..99
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02012"
SQ   SEQUENCE   109 AA;  12643 MW;  AEDC86965A995144 CRC64;
     MSAQPVDIQV FGRSLRVNCP PEQQDALNMA AEDLSQRLQD LKVRTRVNNT EQLVFIAALN
     VCHELAQERL KTRDYASNME QRIRMLQQTI EQALLEQGRI SDRQDTQFE
//
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