ZAPB_ECOLI
ID ZAPB_ECOLI Reviewed; 81 AA.
AC P0AF36; P32164; Q2M8M4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cell division protein ZapB;
GN Name=zapB; Synonyms=yiiU; OrderedLocusNames=b3928, JW3899;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [5]
RP FUNCTION IN CELL DIVISION, COILED-COIL DOMAIN, SUBUNIT, INTERACTION WITH
RP FTSZ, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18394147; DOI=10.1111/j.1365-2958.2008.06190.x;
RA Ebersbach G., Galli E., Moeller-Jensen J., Loewe J., Gerdes K.;
RT "Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and
RT cell division.";
RL Mol. Microbiol. 68:720-735(2008).
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.
CC {ECO:0000269|PubMed:18394147}.
CC -!- SUBUNIT: Homodimer. The ends of the coiled-coil dimer bind to each
CC other, forming polymers. Interacts with FtsZ.
CC {ECO:0000269|PubMed:18394147}.
CC -!- INTERACTION:
CC P0AF36; P0ADS2: zapA; NbExp=4; IntAct=EBI-1134093, EBI-1119901;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18394147}.
CC Note=Localizes to the septum at mid-cell, in a FtsZ-like pattern.
CC -!- SIMILARITY: Belongs to the ZapB family. {ECO:0000305}.
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; L19201; AAB03060.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76910.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77382.1; -; Genomic_DNA.
DR PIR; S40871; S40871.
DR RefSeq; NP_418363.1; NC_000913.3.
DR RefSeq; WP_001296623.1; NZ_STEB01000017.1.
DR PDB; 2JEE; X-ray; 2.80 A; A/B/C/D=1-81.
DR PDBsum; 2JEE; -.
DR AlphaFoldDB; P0AF36; -.
DR SMR; P0AF36; -.
DR BioGRID; 4262648; 241.
DR DIP; DIP-35850N; -.
DR IntAct; P0AF36; 5.
DR STRING; 511145.b3928; -.
DR iPTMnet; P0AF36; -.
DR jPOST; P0AF36; -.
DR PaxDb; P0AF36; -.
DR PRIDE; P0AF36; -.
DR EnsemblBacteria; AAC76910; AAC76910; b3928.
DR EnsemblBacteria; BAE77382; BAE77382; BAE77382.
DR GeneID; 67417561; -.
DR GeneID; 948420; -.
DR KEGG; ecj:JW3899; -.
DR KEGG; eco:b3928; -.
DR PATRIC; fig|511145.12.peg.4046; -.
DR EchoBASE; EB1824; -.
DR eggNOG; COG3074; Bacteria.
DR HOGENOM; CLU_171174_2_0_6; -.
DR OMA; VQSAQHG; -.
DR PhylomeDB; P0AF36; -.
DR BioCyc; EcoCyc:EG11878-MON; -.
DR EvolutionaryTrace; P0AF36; -.
DR PRO; PR:P0AF36; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR HAMAP; MF_01196; ZapB; 1.
DR InterPro; IPR009252; Cell_div_ZapB.
DR Pfam; PF06005; ZapB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Reference proteome; Septation.
FT CHAIN 1..81
FT /note="Cell division protein ZapB"
FT /id="PRO_0000169693"
FT REGION 36..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..81
FT /evidence="ECO:0000255"
FT COMPBIAS 47..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT HELIX 5..78
FT /evidence="ECO:0007829|PDB:2JEE"
SQ SEQUENCE 81 AA; 9635 MW; B01DC1A433A1D01B CRC64;
MTMSLEVFEK LEAKVQQAID TITLLQMEIE ELKEKNNSLS QEVQNAQHQR EELERENNHL
KEQQNGWQER LQALLGRMEE V
