ID A0A085JN98_9GAMM Unreviewed; 79 AA.
AC A0A085JN98;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:KFD21944.1};
GN ORFNames=GTPT_0656 {ECO:0000313|EMBL:KFD21944.1};
OS Tatumella ptyseos ATCC 33301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD21944.1, ECO:0000313|Proteomes:UP000028602};
RN [1] {ECO:0000313|EMBL:KFD21944.1, ECO:0000313|Proteomes:UP000028602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD21944.1,
RC ECO:0000313|Proteomes:UP000028602};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFD21944.1}.
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DR EMBL; JMPR01000011; KFD21944.1; -; Genomic_DNA.
DR RefSeq; WP_025902383.1; NZ_JMPR01000011.1.
DR AlphaFoldDB; A0A085JN98; -.
DR eggNOG; COG3074; Bacteria.
DR OrthoDB; 6554593at2; -.
DR Proteomes; UP000028602; 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 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:UP000028602};
KW Septation {ECO:0000256|HAMAP-Rule:MF_01196}.
FT COILED 6..75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01196"
SQ SEQUENCE 79 AA; 9362 MW; 83D1A380C5EC2E8E CRC64;
MSFEMFEKLE AKVQQAIDTI TLLQMEIEEL KEQNNTLKQE SLQVAGNHDS LTRENQQLKE
EQQQWQERLR ALLGKMDEV
//