ID E8LRY1_9VIBR Unreviewed; 80 AA.
AC E8LRY1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Cell division protein ZapB {ECO:0000256|HAMAP-Rule:MF_01196};
GN Name=zapB {ECO:0000256|HAMAP-Rule:MF_01196};
GN ORFNames=VIBR0546_01203 {ECO:0000313|EMBL:EGA66554.1};
OS Vibrio brasiliensis LMG 20546.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA66554.1, ECO:0000313|Proteomes:UP000004371};
RN [1] {ECO:0000313|EMBL:EGA66554.1, ECO:0000313|Proteomes:UP000004371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA66554.1,
RC ECO:0000313|Proteomes:UP000004371};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01196}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01196}.
CC Note=Localizes to the septum at mid-cell, in a FtsZ-like pattern.
CC {ECO:0000256|HAMAP-Rule:MF_01196}.
CC -!- SIMILARITY: Belongs to the ZapB family. {ECO:0000256|HAMAP-
CC Rule:MF_01196}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGA66554.1}.
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DR EMBL; AEVS01000038; EGA66554.1; -; Genomic_DNA.
DR RefSeq; WP_006878567.1; NZ_AEVS01000038.1.
DR AlphaFoldDB; E8LRY1; -.
DR STRING; 945543.VIBR0546_01203; -.
DR eggNOG; COG3074; Bacteria.
DR Proteomes; UP000004371; Unassembled WGS sequence.
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 Gene3D; 1.20.5.340; -; 1.
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 {ECO:0000256|HAMAP-Rule:MF_01196};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_01196,
KW ECO:0000313|EMBL:EGA66554.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01196}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01196};
KW Septation {ECO:0000256|HAMAP-Rule:MF_01196}.
FT COILED 6..75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01196"
SQ SEQUENCE 80 AA; 9373 MW; C29845FF342464A8 CRC64;
MSFEVLEQLE AKIQTAVDTI ALLQMEVEEL KEEKEKLATE ASELRNSREA LEQQAQQMQQ
EHTAWQERIR NLLGKMDEVE
//
