ID   ZAPB_ECOUT              Reviewed;          81 AA.
AC   Q1R3Z0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Cell division protein ZapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN   Name=zapB {ECO:0000255|HAMAP-Rule:MF_01196}; OrderedLocusNames=UTI89_C4512;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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. Note=Localizes to the septum at mid-
CC       cell, in a FtsZ-like pattern. {ECO:0000255|HAMAP-Rule:MF_01196}.
CC   -!- SIMILARITY: Belongs to the ZapB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01196}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE09924.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000243; ABE09924.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001296623.1; NC_007946.1.
DR   AlphaFoldDB; Q1R3Z0; -.
DR   SMR; Q1R3Z0; -.
DR   EnsemblBacteria; ABE09924; ABE09924; UTI89_C4512.
DR   GeneID; 67417561; -.
DR   KEGG; eci:UTI89_C4512; -.
DR   HOGENOM; CLU_171174_2_0_6; -.
DR   OMA; VQSAQHG; -.
DR   Proteomes; UP000001952; Chromosome.
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..81
FT                   /note="Cell division protein ZapB"
FT                   /id="PRO_0000333899"
FT   REGION          36..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          5..81
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01196"
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:0000255|HAMAP-Rule:MF_01196"
SQ   SEQUENCE   81 AA;  9635 MW;  B01DC1A433A1D01B CRC64;
     MTMSLEVFEK LEAKVQQAID TITLLQMEIE ELKEKNNSLS QEVQNAQHQR EELERENNHL
     KEQQNGWQER LQALLGRMEE V