ID   ZAPB_SHEAM              Reviewed;          67 AA.
AC   A1SAW5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Cell division protein ZapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN   Name=zapB {ECO:0000255|HAMAP-Rule:MF_01196}; OrderedLocusNames=Sama_3319;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
RG   US DOE Joint Genome Institute;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-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; CP000507; ABM01522.1; -; Genomic_DNA.
DR   RefSeq; WP_011761426.1; NC_008700.1.
DR   AlphaFoldDB; A1SAW5; -.
DR   SMR; A1SAW5; -.
DR   STRING; 326297.Sama_3319; -.
DR   EnsemblBacteria; ABM01522; ABM01522; Sama_3319.
DR   KEGG; saz:Sama_3319; -.
DR   eggNOG; COG3074; Bacteria.
DR   HOGENOM; CLU_171174_1_0_6; -.
DR   OMA; VQSAQHG; -.
DR   Proteomes; UP000009175; 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; Reference proteome;
KW   Septation.
FT   CHAIN           1..67
FT                   /note="Cell division protein ZapB"
FT                   /id="PRO_0000333921"
FT   COILED          3..59
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01196"
SQ   SEQUENCE   67 AA;  7577 MW;  47BD949985CC0508 CRC64;
     MSLELLSQLE TKIQTALETI ELLKLELDEE KEKAANLAEQ NHQLKQELSS WNDKITGLVG
     LLSNQVD