ZAPC_ECOLI
ID ZAPC_ECOLI Reviewed; 180 AA.
AC P75862;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cell division protein ZapC {ECO:0000255|HAMAP-Rule:MF_00906};
DE AltName: Full=FtsZ-associated protein C;
DE AltName: Full=Z-ring-associated protein C;
GN Name=zapC {ECO:0000255|HAMAP-Rule:MF_00906}; Synonyms=ycbW;
GN OrderedLocusNames=b0946, JW5125;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 FUNCTION, SUBUNIT, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LEU-22.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21216997; DOI=10.1128/jb.01245-10;
RA Hale C.A., Shiomi D., Liu B., Bernhardt T.G., Margolin W., Niki H.,
RA de Boer P.A.;
RT "Identification of Escherichia coli ZapC (YcbW) as a component of the
RT division apparatus that binds and bundles FtsZ polymers.";
RL J. Bacteriol. 193:1393-1404(2011).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH FTSZ, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=21216995; DOI=10.1128/jb.01258-10;
RA Durand-Heredia J.M., Yu H.H., De Carlo S., Lesser C.F., Janakiraman A.;
RT "Identification and characterization of ZapC, a stabilizer of the FtsZ ring
RT in Escherichia coli.";
RL J. Bacteriol. 193:1405-1413(2011).
CC -!- FUNCTION: Contributes to the efficiency of the cell division process by
CC stabilizing the polymeric form of the cell division protein FtsZ. Acts
CC by promoting interactions between FtsZ protofilaments and suppressing
CC the GTPase activity of FtsZ. {ECO:0000255|HAMAP-Rule:MF_00906,
CC ECO:0000269|PubMed:21216995, ECO:0000269|PubMed:21216997}.
CC -!- SUBUNIT: Interacts directly with FtsZ. Monomer in solution.
CC {ECO:0000255|HAMAP-Rule:MF_00906, ECO:0000269|PubMed:21216995,
CC ECO:0000269|PubMed:21216997}.
CC -!- INTERACTION:
CC P75862; P0A9A6: ftsZ; NbExp=5; IntAct=EBI-552519, EBI-370963;
CC P75862; P0A6Z3: htpG; NbExp=3; IntAct=EBI-552519, EBI-369221;
CC P75862; P75862: zapC; NbExp=3; IntAct=EBI-552519, EBI-552519;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00906,
CC ECO:0000269|PubMed:21216995, ECO:0000269|PubMed:21216997}.
CC Note=Colocalizes with FtsZ at division sites. Localization to the Z
CC ring is dependent on FtsZ and independent of FtsA, ZipA, ZapA or ZapB.
CC -!- DISRUPTION PHENOTYPE: Mutants divide almost normally under standard
CC growth conditions. {ECO:0000269|PubMed:21216997}.
CC -!- SIMILARITY: Belongs to the ZapC family. {ECO:0000255|HAMAP-
CC Rule:MF_00906}.
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DR EMBL; U00096; AAC74032.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35701.2; -; Genomic_DNA.
DR PIR; A64835; A64835.
DR RefSeq; NP_415466.4; NC_000913.3.
DR RefSeq; WP_001295353.1; NZ_SSZK01000002.1.
DR PDB; 5E1L; X-ray; 2.15 A; A=1-180.
DR PDB; 5FO3; X-ray; 2.90 A; A/B=1-180.
DR PDBsum; 5E1L; -.
DR PDBsum; 5FO3; -.
DR AlphaFoldDB; P75862; -.
DR SMR; P75862; -.
DR BioGRID; 4259444; 7.
DR BioGRID; 849926; 21.
DR DIP; DIP-11485N; -.
DR IntAct; P75862; 22.
DR MINT; P75862; -.
DR STRING; 511145.b0946; -.
DR PaxDb; P75862; -.
DR PRIDE; P75862; -.
DR EnsemblBacteria; AAC74032; AAC74032; b0946.
DR EnsemblBacteria; BAA35701; BAA35701; BAA35701.
DR GeneID; 945552; -.
DR KEGG; ecj:JW5125; -.
DR KEGG; eco:b0946; -.
DR PATRIC; fig|1411691.4.peg.1328; -.
DR EchoBASE; EB3479; -.
DR eggNOG; ENOG502Z8AH; Bacteria.
DR HOGENOM; CLU_128248_0_0_6; -.
DR OMA; IKVMNDR; -.
DR PhylomeDB; P75862; -.
DR BioCyc; EcoCyc:G6486-MON; -.
DR PRO; PR:P75862; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036212; P:contractile ring maintenance; IDA:CACAO.
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:0051302; P:regulation of cell division; IMP:EcoliWiki.
DR HAMAP; MF_00906; ZapC; 1.
DR InterPro; IPR009809; ZapC.
DR Pfam; PF07126; ZapC; 1.
DR PIRSF; PIRSF010252; ZapC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Reference proteome;
KW Septation.
FT CHAIN 1..180
FT /note="Cell division protein ZapC"
FT /id="PRO_0000168778"
FT MUTAGEN 22
FT /note="L->P: Does not interact with FtsZ, but shows
FT affinity for itself. Reduces GTPase activity by less than
FT 10%."
FT /evidence="ECO:0000269|PubMed:21216997"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:5E1L"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5E1L"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5E1L"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:5E1L"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5E1L"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5E1L"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5E1L"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5E1L"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5E1L"
SQ SEQUENCE 180 AA; 20589 MW; 7A8CC66ECE2D1B87 CRC64;
MRIKPDDNWR WYYDEEHDRM MLDLANGMLF RSRFARKMLT PDAFSPAGFC VDDAALYFSF
EEKCRDFNLS KEQKAELVLN ALVAIRYLKP QMPKSWHFVS HGEMWVPMPG DAACVWLSDT
HEQVNLLVVE SGENAALCLL AQPCVVIAGR AMQLGDAIKI MNDRLKPQVN VDSFSLEQAV
