ZAPB_ECOLC
ID ZAPB_ECOLC Reviewed; 79 AA.
AC B1IVF1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Cell division protein ZapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN Name=zapB {ECO:0000255|HAMAP-Rule:MF_01196}; OrderedLocusNames=EcolC_4090;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) 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: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 {ECO:0000255|HAMAP-Rule:MF_01196}.
CC Note=Localizes to the septum at mid-cell, in a FtsZ-like pattern.
CC {ECO:0000255|HAMAP-Rule:MF_01196}.
CC -!- SIMILARITY: Belongs to the ZapB family. {ECO:0000255|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; CP000946; ACA79688.1; -; Genomic_DNA.
DR AlphaFoldDB; B1IVF1; -.
DR SMR; B1IVF1; -.
DR KEGG; ecl:EcolC_4090; -.
DR HOGENOM; CLU_171174_2_0_6; -.
DR OMA; VQSAQHG; -.
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 Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm; Septation.
FT CHAIN 1..79
FT /note="Cell division protein ZapB"
FT /id="PRO_1000138434"
FT REGION 34..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..79
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01196"
FT COMPBIAS 45..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01196"
SQ SEQUENCE 79 AA; 9403 MW; A414EC803AE0E05B CRC64;
MSLEVFEKLE AKVQQAIDTI TLLQMEIEEL KEKNNSLSQE VQNAQHQREE LERENNHLKE
QQNGWQERLQ ALLGRMEEV