ID   ZAPB_SHESA              Reviewed;          73 AA.
AC   A0L1Y5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Cell division protein ZapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN   Name=zapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN   OrderedLocusNames=Shewana3_3836;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Non-essential, abundant cell division factor that is required
CC       for proper Z-ring formation. It is recruited early to the divisome by
CC       direct interaction with FtsZ, stimulating Z-ring assembly and thereby
CC       promoting cell division earlier in the cell cycle. Its recruitment to
CC       the Z-ring requires functional FtsA or ZipA. {ECO:0000255|HAMAP-
CC       Rule:MF_01196}.
CC   -!- SUBUNIT: Homodimer. The ends of the coiled-coil dimer bind to each
CC       other, forming polymers. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_01196}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to the septum at mid-
CC       cell, in a FtsZ-like pattern. {ECO:0000255|HAMAP-Rule:MF_01196}.
CC   -!- SIMILARITY: Belongs to the ZapB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01196}.
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; CP000469; ABK50054.1; -; Genomic_DNA.
DR   RefSeq; WP_011718573.1; NC_008577.1.
DR   AlphaFoldDB; A0L1Y5; -.
DR   SMR; A0L1Y5; -.
DR   STRING; 94122.Shewana3_3836; -.
DR   EnsemblBacteria; ABK50054; ABK50054; Shewana3_3836.
DR   KEGG; shn:Shewana3_3836; -.
DR   eggNOG; COG3074; Bacteria.
DR   HOGENOM; CLU_171174_1_0_6; -.
DR   OMA; VQSAQHG; -.
DR   Proteomes; UP000002589; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01196; ZapB; 1.
DR   InterPro; IPR009252; Cell_div_ZapB.
DR   Pfam; PF06005; ZapB; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Septation.
FT   CHAIN           1..73
FT                   /note="Cell division protein ZapB"
FT                   /id="PRO_0000333929"
FT   COILED          3..67
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01196"
SQ   SEQUENCE   73 AA;  8342 MW;  9A1F0F132E8D25ED CRC64;
     MSLELLSKLE TKIQATLETI ELLKMELEEE KQKTSALNEQ NQQLSEQNQQ LQQELASWND
     KVTGLVGLLN SEI