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Database: UniProt
Entry: ZAPA_BACCN
LinkDB: ZAPA_BACCN
Original site: ZAPA_BACCN 
ID   ZAPA_BACCN              Reviewed;          89 AA.
AC   A7GTK4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Cell division protein ZapA {ECO:0000255|HAMAP-Rule:MF_02013};
DE   AltName: Full=Z ring-associated protein ZapA {ECO:0000255|HAMAP-Rule:MF_02013};
GN   Name=zapA {ECO:0000255|HAMAP-Rule:MF_02013}; OrderedLocusNames=Bcer98_3243;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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_02013}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_02013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02013}.
CC       Note=Localizes at mid-cell. In sporulating cells, localizes near the
CC       cell poles. {ECO:0000255|HAMAP-Rule:MF_02013}.
CC   -!- SIMILARITY: Belongs to the ZapA family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02013}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABS23462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000764; ABS23462.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041810059.1; NC_009674.1.
DR   AlphaFoldDB; A7GTK4; -.
DR   SMR; A7GTK4; -.
DR   STRING; 315749.Bcer98_3243; -.
DR   GeneID; 56418786; -.
DR   KEGG; bcy:Bcer98_3243; -.
DR   eggNOG; COG3027; Bacteria.
DR   HOGENOM; CLU_116623_4_0_9; -.
DR   OrthoDB; 9808604at2; -.
DR   Proteomes; UP000002300; 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; 6.10.250.790; -; 1.
DR   HAMAP; MF_02013; ZapA_type2; 1.
DR   InterPro; IPR007838; Cell_div_ZapA-like.
DR   InterPro; IPR036192; Cell_div_ZapA-like_sf.
DR   InterPro; IPR023688; Cell_div_ZapA_firmicutes.
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..89
FT                   /note="Cell division protein ZapA"
FT                   /id="PRO_0000345679"
FT   COILED          64..86
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02013"
SQ   SEQUENCE   89 AA;  10175 MW;  26B977DCD800737E CRC64;
     MSQQKGKKSR INVEIYGQQY SVVGDESTSH IRMVAAIVDD KMRELNAKNP SLDTSRLAVL
     TAVNVIHDYI KLKEEHEKLK ESMRQKGME
//
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