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MINC_ALIF1
ID   MINC_ALIF1              Reviewed;         221 AA.
AC   Q5E447;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Probable septum site-determining protein MinC {ECO:0000255|HAMAP-Rule:MF_00267};
GN   Name=minC {ECO:0000255|HAMAP-Rule:MF_00267}; OrderedLocusNames=VF_1704;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Cell division inhibitor that blocks the formation of polar Z
CC       ring septums. Rapidly oscillates between the poles of the cell to
CC       destabilize FtsZ filaments that have formed before they mature into
CC       polar Z rings. Prevents FtsZ polymerization. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
CC   -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
CC   -!- SIMILARITY: Belongs to the MinC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00267}.
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DR   EMBL; CP000020; AAW86199.1; -; Genomic_DNA.
DR   RefSeq; WP_005420042.1; NC_006840.2.
DR   RefSeq; YP_205087.1; NC_006840.2.
DR   AlphaFoldDB; Q5E447; -.
DR   SMR; Q5E447; -.
DR   STRING; 312309.VF_1704; -.
DR   EnsemblBacteria; AAW86199; AAW86199; VF_1704.
DR   GeneID; 64242211; -.
DR   KEGG; vfi:VF_1704; -.
DR   PATRIC; fig|312309.11.peg.1726; -.
DR   eggNOG; COG0850; Bacteria.
DR   HOGENOM; CLU_067812_0_1_6; -.
DR   OMA; RRDPLWG; -.
DR   OrthoDB; 1665744at2; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0051302; P:regulation of cell division; IEA:InterPro.
DR   GO; GO:1901891; P:regulation of cell septum assembly; IEA:InterPro.
DR   Gene3D; 2.160.20.70; -; 1.
DR   HAMAP; MF_00267; MinC; 1.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR013033; MinC.
DR   InterPro; IPR036145; MinC_C_sf.
DR   InterPro; IPR007874; MinC_N.
DR   InterPro; IPR005526; Septum_form_inhib_MinC_C.
DR   PANTHER; PTHR34108; PTHR34108; 1.
DR   Pfam; PF03775; MinC_C; 1.
DR   Pfam; PF05209; MinC_N; 1.
DR   SUPFAM; SSF63848; SSF63848; 1.
DR   TIGRFAMs; TIGR01222; minC; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Reference proteome; Septation.
FT   CHAIN           1..221
FT                   /note="Probable septum site-determining protein MinC"
FT                   /id="PRO_1000047872"
SQ   SEQUENCE   221 AA;  23892 MW;  B92D0738F29B9E0D CRC64;
     MTKTADLKGS NFTLSVLHLP NDDVALALSM LEQKVAQAPS FFASAPVVVN IENVSNEINF
     VELKSGVERT GMIPVGITGC KDKQKQAQAT AAGFAVMTSF TPQQVTQKAN MQPTKVVKTP
     IRSGQQIYAK DADLVILNHV SPGAEVIADG SIHIHGTLRG RAIAGASGQA EAKVFCKNLQ
     AELISIAGNY WLSDQIDKEY WHQNVMITMV EDRIQIDTLT L
 
 
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