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Database: UniProt
Entry: A0A3N9TBI1_9VIBR
LinkDB: A0A3N9TBI1_9VIBR
Original site: A0A3N9TBI1_9VIBR 
ID   A0A3N9TBI1_9VIBR        Unreviewed;        81 AA.
AC   A0A3N9TBI1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Cell division protein ZapB {ECO:0000256|HAMAP-Rule:MF_01196};
GN   Name=zapB {ECO:0000256|HAMAP-Rule:MF_01196,
GN   ECO:0000313|EMBL:RQW61330.1};
GN   ORFNames=EES38_19660 {ECO:0000313|EMBL:RQW61330.1};
OS   Vibrio viridaestus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2487322 {ECO:0000313|EMBL:RQW61330.1, ECO:0000313|Proteomes:UP000281112};
RN   [1] {ECO:0000313|EMBL:RQW61330.1, ECO:0000313|Proteomes:UP000281112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LJC006 {ECO:0000313|EMBL:RQW61330.1,
RC   ECO:0000313|Proteomes:UP000281112};
RA   Liang J.;
RT   "Vibrio LJC006 sp. nov., isolated from seawater during the bloom of the
RT   enteromorpha.";
RL   Submitted (NOV-2018) 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: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:RQW61330.1}.
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DR   EMBL; RJVQ01000013; RQW61330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N9TBI1; -.
DR   OrthoDB; 6554593at2; -.
DR   Proteomes; UP000281112; 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:RQW61330.1};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   Rule:MF_01196}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01196};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281112};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_01196}.
FT   COILED          6..68
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01196"
SQ   SEQUENCE   81 AA;  9530 MW;  5755BEDB0C268033 CRC64;
     MSFEVLEQLE AKIQTAVDTI TLLQMEVEEL KEDKQKLESE ANELRTSREE LEQRVQTIQQ
     EHAAWQERIR SLIGKMDNVE S
//
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