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ZAPD_BORPD
ID   ZAPD_BORPD              Reviewed;         250 AA.
AC   A9I1I9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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}; OrderedLocusNames=Bpet0534;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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}.
CC   -!- SUBUNIT: Interacts with FtsZ. {ECO:0000255|HAMAP-Rule:MF_01092}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01092}.
CC       Note=Localizes to mid-cell in an FtsZ-dependent manner.
CC       {ECO:0000255|HAMAP-Rule:MF_01092}.
CC   -!- SIMILARITY: Belongs to the ZapD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01092}.
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DR   EMBL; AM902716; CAP40866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9I1I9; -.
DR   SMR; A9I1I9; -.
DR   STRING; 94624.Bpet0534; -.
DR   EnsemblBacteria; CAP40866; CAP40866; Bpet0534.
DR   KEGG; bpt:Bpet0534; -.
DR   eggNOG; COG4582; Bacteria.
DR   OMA; LPAYYAW; -.
DR   Proteomes; UP000001225; 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   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   3: Inferred from homology;
KW   Cell cycle; Cell division; Cytoplasm; Reference proteome; Septation.
FT   CHAIN           1..250
FT                   /note="Cell division protein ZapD"
FT                   /id="PRO_1000136927"
SQ   SEQUENCE   250 AA;  28473 MW;  9F2B166BD507472A CRC64;
     MILYEYPFNE RVRAYLRLEY LFDRLFYFAR EGDARHHQIA VATLFDILDA TERTDIKTSV
     LQDLERQRAA LQALRDHPGV AQDALESMLA EMERTVSGLA GQGRAGQPLR ENEWLVSLRG
     RLAVPGGATQ VDMPSYHAWQ HRTEAVRCAD LQTWTAPLRP LHDAVAMALR LLRESGRRSE
     IVAEQGGYQQ MLAGKLFQLL RVWIDPAQGV FPEISANKYM IWIRFSAQDG DAKPQQVARN
     IDFQMSLCSS
 
 
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