ZIPA_ECOLI
ID ZIPA_ECOLI Reviewed; 328 AA.
AC P77173;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509};
DE AltName: Full=FtsZ interacting protein A {ECO:0000303|PubMed:9008158};
GN Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509, ECO:0000303|PubMed:9008158};
GN OrderedLocusNames=b2412, JW2404;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH FTSZ,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=PB103;
RX PubMed=9008158; DOI=10.1016/s0092-8674(00)81838-3;
RA Hale C.A., de Boer P.A.J.;
RT "Direct binding of FtsZ to ZipA, an essential component of the septal ring
RT structure that mediates cell division in E. coli.";
RL Cell 88:175-185(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9864327; DOI=10.1128/jb.181.1.167-176.1999;
RA Hale C.A., de Boer P.A.;
RT "Recruitment of ZipA to the septal ring of Escherichia coli is dependent on
RT FtsZ and independent of FtsA.";
RL J. Bacteriol. 181:167-176(1999).
RN [6]
RP FUNCTION, INTERACTION WITH FTSZ, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=10209756; DOI=10.1046/j.1365-2958.1999.01322.x;
RA Liu Z., Mukherjee A., Lutkenhaus J.;
RT "Recruitment of ZipA to the division site by interaction with FtsZ.";
RL Mol. Microbiol. 31:1853-1861(1999).
RN [7]
RP FUNCTION IN Z RING ASSEMBLY, AND FUNCTION IN RECRUITMENT OF FTSK.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11847116; DOI=10.1093/emboj/21.4.685;
RA Pichoff S., Lutkenhaus J.;
RT "Unique and overlapping roles for ZipA and FtsA in septal ring assembly in
RT Escherichia coli.";
RL EMBO J. 21:685-693(2002).
RN [8]
RP FUNCTION IN RECRUITMENT OF CELL DIVISION PROTEINS.
RX PubMed=11948172; DOI=10.1128/jb.184.9.2552-2556.2002;
RA Hale C.A., de Boer P.A.J.;
RT "ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the
RT septal ring in Escherichia coli.";
RL J. Bacteriol. 184:2552-2556(2002).
RN [9]
RP DOMAIN.
RX PubMed=12107152; DOI=10.1128/jb.184.15.4313-4315.2002;
RA Ohashi T., Hale C.A., de Boer P.A., Erickson H.P.;
RT "Structural evidence that the P/Q domain of ZipA is an unstructured,
RT flexible tether between the membrane and the C-terminal FtsZ-binding
RT domain.";
RL J. Bacteriol. 184:4313-4315(2002).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [11]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [12]
RP FUNCTION, AND INTERACTION WITH FTSZ.
RX PubMed=22164258; DOI=10.1371/journal.pone.0028262;
RA Kuchibhatla A., Bhattacharya A., Panda D.;
RT "ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ
RT protofilaments.";
RL PLoS ONE 6:E28262-E28262(2011).
RN [13]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22304478; DOI=10.1021/bi2015647;
RA Skoog K., Daley D.O.;
RT "The Escherichia coli cell division protein ZipA forms homodimers prior to
RT association with FtsZ.";
RL Biochemistry 51:1407-1415(2012).
RN [14]
RP FUNCTION.
RX PubMed=23233671; DOI=10.1074/jbc.m112.434944;
RA Pazos M., Natale P., Vicente M.;
RT "A specific role for the ZipA protein in cell division: stabilization of
RT the FtsZ protein.";
RL J. Biol. Chem. 288:3219-3226(2013).
RN [15] {ECO:0007744|PDB:1F7W, ECO:0007744|PDB:1F7X}
RP STRUCTURE BY NMR OF 185-328.
RX PubMed=10924108; DOI=10.1021/bi0009690;
RA Moy F.J., Glasfeld E., Mosyak L., Powers R.;
RT "Solution structure of ZipA, a crucial component of Escherichia coli cell
RT division.";
RL Biochemistry 39:9146-9156(2000).
RN [16] {ECO:0007744|PDB:1F46, ECO:0007744|PDB:1F47}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 189-328, AND INTERACTION WITH
RP FTSZ.
RX PubMed=10880432; DOI=10.1093/emboj/19.13.3179;
RA Mosyak L., Zhang Y., Glasfeld E., Haney S., Stahl M., Seehra J.,
RA Somers W.S.;
RT "The bacterial cell-division protein ZipA and its interaction with an FtsZ
RT fragment revealed by X-ray crystallography.";
RL EMBO J. 19:3179-3191(2000).
RN [17] {ECO:0007744|PDB:1S1J, ECO:0007744|PDB:1S1S}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 185-328.
RX PubMed=15006376; DOI=10.1016/j.bmcl.2004.01.028;
RA Jennings L.D., Foreman K.W., Rush T.S. III, Tsao D.H., Mosyak L., Li Y.,
RA Sukhdeo M.N., Ding W., Dushin E.G., Kenny C.H., Moghazeh S.L.,
RA Petersen P.J., Ruzin A.V., Tuckman M., Sutherland A.G.;
RT "Design and synthesis of indolo[2,3-a]quinolizin-7-one inhibitors of the
RT ZipA-FtsZ interaction.";
RL Bioorg. Med. Chem. Lett. 14:1427-1431(2004).
RN [18] {ECO:0007744|PDB:1Y2F, ECO:0007744|PDB:1Y2G}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 189-328.
RX PubMed=15743191; DOI=10.1021/jm040163o;
RA Rush T.S. III, Grant J.A., Mosyak L., Nicholls A.;
RT "A shape-based 3-D scaffold hopping method and its application to a
RT bacterial protein-protein interaction.";
RL J. Med. Chem. 48:1489-1495(2005).
CC -!- FUNCTION: Essential cell division protein that stabilizes the FtsZ
CC protofilaments by cross-linking them and that serves as a cytoplasmic
CC membrane anchor for the Z ring (PubMed:9008158, PubMed:11847116,
CC PubMed:22164258, PubMed:22304478, PubMed:23233671). Also required for
CC the recruitment to the septal ring of the downstream cell division
CC proteins FtsK, FtsQ, FtsL and FtsN (PubMed:11847116, PubMed:11948172).
CC ZipA overproduction protects FtsZ from degradation by ClpP by
CC preventing recognition by ClpX (PubMed:23233671). Does not affect the
CC GTPase activity of FtsZ (PubMed:10209756).
CC {ECO:0000269|PubMed:10209756, ECO:0000269|PubMed:11847116,
CC ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:22164258,
CC ECO:0000269|PubMed:22304478, ECO:0000269|PubMed:23233671,
CC ECO:0000269|PubMed:9008158}.
CC -!- SUBUNIT: Interacts with FtsZ via their C-terminal domains
CC (PubMed:9008158, PubMed:10209756, PubMed:10880432, PubMed:22164258).
CC Can form homodimers prior to association with FtsZ (PubMed:22304478).
CC {ECO:0000269|PubMed:10209756, ECO:0000269|PubMed:10880432,
CC ECO:0000269|PubMed:22164258, ECO:0000269|PubMed:22304478,
CC ECO:0000269|PubMed:9008158}.
CC -!- INTERACTION:
CC P77173; P0A9A6: ftsZ; NbExp=5; IntAct=EBI-1029213, EBI-370963;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:9008158}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:9008158}. Note=Localizes to the Z ring in an FtsZ-
CC dependent manner (PubMed:9008158, PubMed:9864327, PubMed:10209756).
CC Localization does not depend upon FtsA or FtsI (PubMed:9864327,
CC PubMed:10209756). {ECO:0000269|PubMed:10209756,
CC ECO:0000269|PubMed:9008158, ECO:0000269|PubMed:9864327}.
CC -!- INDUCTION: Repressed 1.5-fold by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC -!- DOMAIN: Contains an N-terminal transmembrane domain, followed by a
CC charged domain, an unstructured P/Q domain rich in proline and
CC glutamine, and a C-terminal FtsZ-binding domain.
CC {ECO:0000305|PubMed:12107152}.
CC -!- MISCELLANEOUS: Has been isolated as a 91 kDa complex containing ZipA-
CC EptA and an unidentified 24 kDa protein (PubMed:16079137), but it was
CC shown later that there is no physical interaction between ZipA and EptA
CC (PubMed:22304478). {ECO:0000305|PubMed:16079137,
CC ECO:0000305|PubMed:22304478}.
CC -!- SIMILARITY: Belongs to the ZipA family. {ECO:0000255|HAMAP-
CC Rule:MF_00509, ECO:0000305}.
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DR EMBL; U74650; AAB42061.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75465.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16284.1; -; Genomic_DNA.
DR PIR; C65015; C65015.
DR RefSeq; NP_416907.1; NC_000913.3.
DR RefSeq; WP_001300494.1; NZ_LN832404.1.
DR PDB; 1F46; X-ray; 1.50 A; A/B=189-328.
DR PDB; 1F47; X-ray; 1.95 A; B=185-328.
DR PDB; 1F7W; NMR; -; A=185-328.
DR PDB; 1F7X; NMR; -; A=185-328.
DR PDB; 1S1J; X-ray; 2.18 A; A/B=185-328.
DR PDB; 1S1S; X-ray; 2.10 A; A/B=185-328.
DR PDB; 1Y2F; X-ray; 2.00 A; A=190-328.
DR PDB; 1Y2G; X-ray; 1.90 A; A/B=189-328.
DR PDBsum; 1F46; -.
DR PDBsum; 1F47; -.
DR PDBsum; 1F7W; -.
DR PDBsum; 1F7X; -.
DR PDBsum; 1S1J; -.
DR PDBsum; 1S1S; -.
DR PDBsum; 1Y2F; -.
DR PDBsum; 1Y2G; -.
DR AlphaFoldDB; P77173; -.
DR SMR; P77173; -.
DR BioGRID; 4261708; 561.
DR BioGRID; 851209; 1.
DR ComplexPortal; CPX-1936; Divisome complex.
DR DIP; DIP-1157N; -.
DR IntAct; P77173; 2.
DR STRING; 511145.b2412; -.
DR BindingDB; P77173; -.
DR ChEMBL; CHEMBL3954; -.
DR DrugBank; DB02191; (7as,12ar,12bs)-1,2,3,4,7a,12,12a,12b-Octahydroindolo[2,3-a]Quinolizin-7(6h)-One.
DR DrugBank; DB03916; 4-{2-[4-(2-Aminoethyl)Piperazin-1-Yl]Pyridin-4-Yl}-N-(3-Chloro-4-Methylphenyl)Pyrimidin-2-Amine.
DR DrugBank; DB04154; N-Methyl-N-[3-(6-Phenyl[1,2,4]Triazolo[4,3-B]Pyridazin-3-Yl)Phenyl]Acetamide.
DR DrugBank; DB01967; N-{3-[(7ar,12as,12bs)-7-Oxo-1,3,4,6,7,7a,12a,12b-Octahydroindolo[2,3-a]Quinolizin-12(2h)-Yl]Propyl}Propane-2-Sulfonamide.
DR jPOST; P77173; -.
DR PaxDb; P77173; -.
DR PRIDE; P77173; -.
DR EnsemblBacteria; AAC75465; AAC75465; b2412.
DR EnsemblBacteria; BAA16284; BAA16284; BAA16284.
DR GeneID; 946869; -.
DR KEGG; ecj:JW2404; -.
DR KEGG; eco:b2412; -.
DR PATRIC; fig|511145.12.peg.2506; -.
DR EchoBASE; EB3921; -.
DR eggNOG; COG3115; Bacteria.
DR HOGENOM; CLU_030174_1_0_6; -.
DR InParanoid; P77173; -.
DR OMA; FWSIRKQ; -.
DR PhylomeDB; P77173; -.
DR BioCyc; EcoCyc:G7258-MON; -.
DR EvolutionaryTrace; P77173; -.
DR PRO; PR:P77173; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR GO; GO:1990586; C:divisome complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0051301; P:cell division; IC:ComplexPortal.
DR GO; GO:0000917; P:division septum assembly; IMP:EcoliWiki.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IC:ComplexPortal.
DR CDD; cd00231; ZipA; 1.
DR DisProt; DP00161; -.
DR Gene3D; 3.30.1400.10; -; 1.
DR HAMAP; MF_00509; ZipA; 1.
DR InterPro; IPR011919; Cell_div_ZipA.
DR InterPro; IPR007449; ZipA_FtsZ-bd_C.
DR InterPro; IPR036765; ZipA_FtsZ-bd_C_sf.
DR PANTHER; PTHR38685; PTHR38685; 1.
DR Pfam; PF04354; ZipA_C; 1.
DR SMART; SM00771; ZipA_C; 1.
DR SUPFAM; SSF64383; SSF64383; 1.
DR TIGRFAMs; TIGR02205; septum_zipA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..328
FT /note="Cell division protein ZipA"
FT /id="PRO_0000214521"
FT TOPO_DOM 1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509,
FT ECO:0000269|PubMed:9008158"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509"
FT TOPO_DOM 28..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00509,
FT ECO:0000269|PubMed:9008158"
FT REGION 42..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 211
FT /note="L -> A (in Ref. 1; AAB42061)"
FT /evidence="ECO:0000305"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:1F46"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:1F46"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1F46"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1F46"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:1F46"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:1F46"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:1F7W"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:1F46"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1F46"
FT HELIX 278..296
FT /evidence="ECO:0007829|PDB:1F46"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1F46"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1S1S"
FT HELIX 310..326
FT /evidence="ECO:0007829|PDB:1F46"
SQ SEQUENCE 328 AA; 36475 MW; A20F119A153A782B CRC64;
MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD DSYDEDVEDD
EGVGEVRVHR VNHAPANAQE HEAARPSPQH QYQPPYASAQ PRQPVQQPPE AQVPPQHAPH
PAQPVQQPAY QPQPEQPLQQ PVSPQVAPAP QPVHSAPQPA QQAFQPAEPV AAPQPEPVAE
PAPVMDKPKR KEAVIIMNVA AHHGSELNGE LLLNSIQQAG FIFGDMNIYH RHLSPDGSGP
ALFSLANMVK PGTFDPEMKD FTTPGVTIFM QVPSYGDELQ NFKLMLQSAQ HIADEVGGVV
LDDQRRMMTP QKLREYQDII REVKDANA
