ZAPB_PECCP
ID ZAPB_PECCP Reviewed; 79 AA.
AC C6DHM3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Cell division protein ZapB {ECO:0000255|HAMAP-Rule:MF_01196};
GN Name=zapB {ECO:0000255|HAMAP-Rule:MF_01196}; OrderedLocusNames=PC1_0162;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT11223.1; -; Genomic_DNA.
DR RefSeq; WP_010281529.1; NC_012917.1.
DR AlphaFoldDB; C6DHM3; -.
DR SMR; C6DHM3; -.
DR STRING; 561230.PC1_0162; -.
DR EnsemblBacteria; ACT11223; ACT11223; PC1_0162.
DR GeneID; 61410041; -.
DR KEGG; pct:PC1_0162; -.
DR eggNOG; COG3074; Bacteria.
DR HOGENOM; CLU_171174_2_0_6; -.
DR OMA; VQSAQHG; -.
DR OrthoDB; 2065751at2; -.
DR Proteomes; UP000002736; 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 Cell cycle; Cell division; Coiled coil; Cytoplasm; Septation.
FT CHAIN 1..79
FT /note="Cell division protein ZapB"
FT /id="PRO_1000213805"
FT COILED 4..78
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01196"
SQ SEQUENCE 79 AA; 9131 MW; 5BDB8A1E508FE714 CRC64;
MSFEVFEKLE AKVQQAIDTI TLLQMEIEEL KEQNNALSQD VQAAAGSREA LVRENEQLKE
EQVVWQERLR ALLGKMEEV