ID   ZAPA_BACSU              Reviewed;          85 AA.
AC   P94542; Q795X2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Cell division protein ZapA;
DE   AltName: Full=Z ring-associated protein ZapA;
GN   Name=zapA; Synonyms=yshA; OrderedLocusNames=BSU28610;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION IN ASSEMBLY OF Z RING, INTERACTION WITH FTSZ, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168 / PY79;
RX   PubMed=12368265; DOI=10.1101/gad.1014102;
RA   Gueiros-Filho F.J., Losick R.;
RT   "A widely conserved bacterial cell division protein that promotes assembly
RT   of the tubulin-like protein FtsZ.";
RL   Genes Dev. 16:2544-2556(2002).
RN   [4]
RP   INTERACTION WITH FTSZ.
RC   STRAIN=168 / PY79;
RX   PubMed=15317782; DOI=10.1128/jb.186.17.5775-5781.2004;
RA   Anderson D.E., Gueiros-Filho F.J., Erickson H.P.;
RT   "Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli
RT   and effects of FtsZ-regulating proteins.";
RL   J. Bacteriol. 186:5775-5781(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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:12368265}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P94542; P17865: ftsZ; NbExp=4; IntAct=EBI-2122911, EBI-1569853;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes at mid-
CC       cell. In sporulating cells, localizes near the cell poles (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ZapA family. Type 2 subfamily.
CC       {ECO:0000305}.
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; Z75208; CAA99566.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14821.1; -; Genomic_DNA.
DR   PIR; A69985; A69985.
DR   RefSeq; NP_390739.1; NC_000964.3.
DR   RefSeq; WP_003229534.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P94542; -.
DR   SMR; P94542; -.
DR   IntAct; P94542; 8.
DR   STRING; 224308.BSU28610; -.
DR   PaxDb; P94542; -.
DR   PRIDE; P94542; -.
DR   EnsemblBacteria; CAB14821; CAB14821; BSU_28610.
DR   GeneID; 937442; -.
DR   KEGG; bsu:BSU28610; -.
DR   PATRIC; fig|224308.179.peg.3108; -.
DR   eggNOG; COG3027; Bacteria.
DR   InParanoid; P94542; -.
DR   OMA; KMHEFSE; -.
DR   PhylomeDB; P94542; -.
DR   BioCyc; BSUB:BSU28610-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0000917; P:division septum assembly; IBA:GO_Central.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IBA:GO_Central.
DR   GO; GO:0000921; P:septin ring assembly; IBA:GO_Central.
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; PTHR34981; 1.
DR   Pfam; PF05164; ZapA; 1.
DR   SUPFAM; SSF102829; SSF102829; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Reference proteome;
KW   Septation.
FT   CHAIN           1..85
FT                   /note="Cell division protein ZapA"
FT                   /id="PRO_0000345674"
FT   COILED          58..85
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   85 AA;  9866 MW;  7B08728296B16045 CRC64;
     MSDGKKTKTT VDIYGQHFTI VGEESRAHMR YVAGIVDDKM REINEKNPYL DINKLAVLTA
     VNVVHDYVKL QEKCEKLERQ LKEKD