GenomeNet

Database: UniProt
Entry: A0A1B1E925_VIBNA
LinkDB: A0A1B1E925_VIBNA
Original site: A0A1B1E925_VIBNA 
ID   A0A1B1E925_VIBNA        Unreviewed;        80 AA.
AC   A0A1B1E925;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Cell division protein ZapB {ECO:0000256|HAMAP-Rule:MF_01196};
GN   Name=zapB {ECO:0000256|HAMAP-Rule:MF_01196};
GN   ORFNames=BA894_01740 {ECO:0000313|EMBL:ANQ25251.1};
OS   Vibrio natriegens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=691 {ECO:0000313|EMBL:ANQ25251.1, ECO:0000313|Proteomes:UP000092577};
RN   [1] {ECO:0000313|EMBL:ANQ25251.1, ECO:0000313|Proteomes:UP000092577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 16374 {ECO:0000313|EMBL:ANQ25251.1,
RC   ECO:0000313|Proteomes:UP000092577};
RA   Weinstock M.T., Hesek E.D., Wilson C.M., Gibson D.G.;
RT   "Developing Vibrio natriegens as a novel, fast-growing host for
RT   biotechnology.";
RL   Submitted (JUL-2016) 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   ---------------------------------------------------------------------------
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; CP016351; ANQ25251.1; -; Genomic_DNA.
DR   RefSeq; WP_014230654.1; NZ_SZTN01000003.1.
DR   AlphaFoldDB; A0A1B1E925; -.
DR   STRING; 691.BA893_01495; -.
DR   GeneID; 70913545; -.
DR   Proteomes; UP000092577; Chromosome 1.
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   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;  9396 MW;  E7C15D55008FE75A CRC64;
     MSFEVLAQLE SKIQTAVDTI TLLQMEVEEL KEDKVKLEAQ ANELRTQREE LEQKAEQAQQ
     EHAQWQERIR ALLGKMEEVE
//
DBGET integrated database retrieval system