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MINC_PARP8
ID   MINC_PARP8              Reviewed;         282 AA.
AC   B2JEG8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Bphy_0655;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC69845.1; -; Genomic_DNA.
DR   RefSeq; WP_012400066.1; NZ_CADFGH010000020.1.
DR   AlphaFoldDB; B2JEG8; -.
DR   SMR; B2JEG8; -.
DR   STRING; 391038.Bphy_0655; -.
DR   EnsemblBacteria; ACC69845; ACC69845; Bphy_0655.
DR   KEGG; bph:Bphy_0655; -.
DR   eggNOG; COG0850; Bacteria.
DR   HOGENOM; CLU_067812_0_0_4; -.
DR   OMA; RRDPLWG; -.
DR   OrthoDB; 1665744at2; -.
DR   Proteomes; UP000001192; Chromosome 1.
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..282
FT                   /note="Probable septum site-determining protein MinC"
FT                   /id="PRO_1000114273"
FT   REGION          95..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   282 AA;  30171 MW;  818C096F3B70A190 CRC64;
     MSPRKSPFFE LRSGAVDTLL FVVKTTDLAE MRAELTRRFE ATPEFFANDT VAIDVRRLAE
     NERVPLAEIA TLLGSVRMRP IGVVADSTQH GWANEAGLPL LDARDPRGGR NHGDEAGEEA
     PGKPGAVAPK PDAAPPADAA SNAQVQMQLP IAAQEDGAPQ AAAEGVRIGT SSQTTVIDKP
     LRSGQRIYAK GDLVVLGMVS NGAEVIAEGN IHIYAPLRGR ALAGVHGNHD ARIFCTCLEA
     ELISIAGIYR TTENPLPADV HGKPVQIWLD EEKLMIEPLR LT
 
 
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