ID   ZAPB_KLEP3              Reviewed;          81 AA.
AC   B5XTD6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Cell division protein ZapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN   Name=zapB {ECO:0000255|HAMAP-Rule:MF_01196}; OrderedLocusNames=KPK_0087;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(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. {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}.
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DR   EMBL; CP000964; ACI07703.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XTD6; -.
DR   SMR; B5XTD6; -.
DR   EnsemblBacteria; ACI07703; ACI07703; KPK_0087.
DR   KEGG; kpe:KPK_0087; -.
DR   HOGENOM; CLU_171174_2_0_6; -.
DR   OMA; VQSAQHG; -.
DR   Proteomes; UP000001734; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   HAMAP; MF_01196; ZapB; 1.
DR   InterPro; IPR009252; Cell_div_ZapB.
DR   InterPro; IPR010989; SNARE.
DR   Pfam; PF06005; ZapB; 1.
DR   SUPFAM; SSF47661; SSF47661; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Septation.
FT   CHAIN           1..81
FT                   /note="Cell division protein ZapB"
FT                   /id="PRO_1000138441"
FT   REGION          43..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          5..81
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01196"
SQ   SEQUENCE   81 AA;  9543 MW;  CD29F153CDA9C751 CRC64;
     MTMSLEVFEK LESKVQQAID TITLLQMEIE ELKEKNNTLV QEVQSAQHGR EELERENSQL
     KEQQQGWQDR LQALLGRMEE V