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 27-MAR-2024, entry version 102.
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; Pseudomonadota; 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 KEGG; vfi:VF_1704; -.
DR PATRIC; fig|312309.11.peg.1726; -.
DR eggNOG; COG0850; Bacteria.
DR HOGENOM; CLU_067812_0_1_6; -.
DR OrthoDB; 9794530at2; -.
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 Gene3D; 3.30.70.260; -; 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 NCBIfam; TIGR01222; minC; 1.
DR PANTHER; PTHR34108; SEPTUM SITE-DETERMINING PROTEIN MINC; 1.
DR PANTHER; PTHR34108:SF1; SEPTUM SITE-DETERMINING PROTEIN MINC; 1.
DR Pfam; PF03775; MinC_C; 1.
DR Pfam; PF05209; MinC_N; 1.
DR SUPFAM; SSF63848; Cell-division inhibitor MinC, C-terminal domain; 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
//
