ID   ZAPB_VIBC3              Reviewed;          80 AA.
AC   A5F4W4; C3LXT4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Cell division protein ZapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN   Name=zapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN   OrderedLocusNames=VC0395_A2259, VC395_2799;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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}.
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DR   EMBL; CP000627; ABQ21989.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP10784.1; -; Genomic_DNA.
DR   RefSeq; WP_000007388.1; NZ_JAACZH010000007.1.
DR   AlphaFoldDB; A5F4W4; -.
DR   SMR; A5F4W4; -.
DR   STRING; 345073.VC395_2799; -.
DR   EnsemblBacteria; ABQ21989; ABQ21989; VC0395_A2259.
DR   GeneID; 57991067; -.
DR   KEGG; vco:VC0395_A2259; -.
DR   KEGG; vcr:VC395_2799; -.
DR   PATRIC; fig|345073.21.peg.2697; -.
DR   eggNOG; COG3074; Bacteria.
DR   HOGENOM; CLU_171174_2_0_6; -.
DR   OMA; VQSAQHG; -.
DR   Proteomes; UP000000249; Chromosome 2.
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..80
FT                   /note="Cell division protein ZapB"
FT                   /id="PRO_0000333939"
FT   COILED          3..80
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01196"
SQ   SEQUENCE   80 AA;  9421 MW;  E9995C0E5DFAD468 CRC64;
     MSFEVLEKLE AKIQTAVDTI ALLQMEVEEL KEEKQQLQNE AQELREAREA LEQRAQQVQQ
     EHAAWQERIR SLLGKMEDVE