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ZAPD_ECOLI
ID   ZAPD_ECOLI              Reviewed;         247 AA.
AC   P36680; P75645; Q8KJQ6; Q8KMZ7;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Cell division protein ZapD {ECO:0000255|HAMAP-Rule:MF_01092};
DE   AltName: Full=Z ring-associated protein D {ECO:0000255|HAMAP-Rule:MF_01092};
GN   Name=zapD {ECO:0000255|HAMAP-Rule:MF_01092}; Synonyms=yacF;
GN   OrderedLocusNames=b0102, JW0099;
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=8202364; DOI=10.1093/nar/22.9.1637;
RA   Fujita N., Mori H., Yura T., Ishihama A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT   4.1 min (110,917-193,643 bp) region.";
RL   Nucleic Acids Res. 22:1637-1639(1994).
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], AND SEQUENCE REVISION.
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 GENE NAME.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=22505682; DOI=10.1128/jb.00176-12;
RA   Durand-Heredia J., Rivkin E., Fan G., Morales J., Janakiraman A.;
RT   "Identification of ZapD as a cell division factor that promotes the
RT   assembly of FtsZ in Escherichia coli.";
RL   J. Bacteriol. 194:3189-3198(2012).
CC   -!- FUNCTION: Cell division factor that enhances FtsZ-ring assembly.
CC       Directly interacts with FtsZ and promotes bundling of FtsZ
CC       protofilaments, with a reduction in FtsZ GTPase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01092, ECO:0000269|PubMed:22505682}.
CC   -!- SUBUNIT: Mostly homodimer in solution. Interacts with the C-terminal
CC       tail of FtsZ. {ECO:0000269|PubMed:22505682}.
CC   -!- INTERACTION:
CC       P36680; P0A9A6: ftsZ; NbExp=3; IntAct=EBI-1113728, EBI-370963;
CC       P36680; P36680: zapD; NbExp=2; IntAct=EBI-1113728, EBI-1113728;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01092,
CC       ECO:0000269|PubMed:22505682}. Note=Localizes to mid-cell in an FtsZ-
CC       dependent manner. Localization does not require FtsA, ZipA, ZapA or
CC       ZapC.
CC   -!- DISRUPTION PHENOTYPE: Mutants are viable, with no discernible division
CC       phenotypes. {ECO:0000269|PubMed:22505682}.
CC   -!- SIMILARITY: Belongs to the ZapD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01092}.
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DR   EMBL; U00096; AAC73213.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96671.2; -; Genomic_DNA.
DR   PIR; F64732; F64732.
DR   RefSeq; NP_414644.1; NC_000913.3.
DR   RefSeq; WP_001194734.1; NZ_STEB01000010.1.
DR   PDB; 5DKO; X-ray; 2.40 A; A=1-247.
DR   PDB; 5IMJ; X-ray; 3.10 A; A/B=2-247.
DR   PDB; 5KOA; X-ray; 2.67 A; A/B=2-247.
DR   PDBsum; 5DKO; -.
DR   PDBsum; 5IMJ; -.
DR   PDBsum; 5KOA; -.
DR   AlphaFoldDB; P36680; -.
DR   SMR; P36680; -.
DR   BioGRID; 4260784; 3.
DR   IntAct; P36680; 5.
DR   STRING; 511145.b0102; -.
DR   jPOST; P36680; -.
DR   PaxDb; P36680; -.
DR   PRIDE; P36680; -.
DR   EnsemblBacteria; AAC73213; AAC73213; b0102.
DR   EnsemblBacteria; BAB96671; BAB96671; BAB96671.
DR   GeneID; 66671609; -.
DR   GeneID; 944873; -.
DR   KEGG; ecj:JW0099; -.
DR   KEGG; eco:b0102; -.
DR   PATRIC; fig|1411691.4.peg.2179; -.
DR   EchoBASE; EB2219; -.
DR   eggNOG; COG4582; Bacteria.
DR   HOGENOM; CLU_076303_0_0_6; -.
DR   OMA; LPAYYAW; -.
DR   PhylomeDB; P36680; -.
DR   BioCyc; EcoCyc:EG12313-MON; -.
DR   PRO; PR:P36680; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR   Gene3D; 2.60.440.10; -; 1.
DR   HAMAP; MF_01092; ZapD; 1.
DR   InterPro; IPR009777; ZapD.
DR   InterPro; IPR027462; ZapD_C.
DR   InterPro; IPR036268; ZapD_sf.
DR   PANTHER; PTHR39455; PTHR39455; 1.
DR   Pfam; PF07072; ZapD; 1.
DR   SUPFAM; SSF160950; SSF160950; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm; Reference proteome;
KW   Septation.
FT   CHAIN           1..247
FT                   /note="Cell division protein ZapD"
FT                   /id="PRO_0000211667"
FT   CONFLICT        215
FT                   /note="I -> T (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..12
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           13..28
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           37..55
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           59..76
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           85..104
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           110..114
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           116..124
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   TURN            128..131
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           137..142
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           147..159
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           162..175
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   STRAND          182..187
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   STRAND          199..204
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   STRAND          211..218
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   STRAND          221..233
FT                   /evidence="ECO:0007829|PDB:5DKO"
FT   STRAND          240..246
FT                   /evidence="ECO:0007829|PDB:5DKO"
SQ   SEQUENCE   247 AA;  28292 MW;  3C0B917A7FA844AC CRC64;
     MQTQVLFEHP LNEKMRTWLR IEFLIQQLTV NLPIVDHAGA LHFFRNVSEL LDVFERGEVR
     TELLKELDRQ QRKLQTWIGV PGVDQSRIEA LIQQLKAAGS VLISAPRIGQ FLREDRLIAL
     VRQRLSIPGG CCSFDLPTLH IWLHLPQAQR DSQVETWIAS LNPLTQALTM VLDLIRQSAP
     FRKQTSLNGF YQDNGGDADL LRLNLSLDSQ LYPQISGHKS RFAIRFMPLD TENGQVPERL
     DFELACC
 
 
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