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Database: UniProt
Entry: A0A220U4I0_9BACI
LinkDB: A0A220U4I0_9BACI
Original site: A0A220U4I0_9BACI 
ID   A0A220U4I0_9BACI        Unreviewed;       228 AA.
AC   A0A220U4I0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   18-JUN-2025, entry version 30.
DE   RecName: Full=Probable septum site-determining protein MinC {ECO:0000256|HAMAP-Rule:MF_00267};
GN   Name=minC {ECO:0000256|HAMAP-Rule:MF_00267};
GN   ORFNames=CFK37_13390 {ECO:0000313|EMBL:ASK63068.1};
OS   Virgibacillus phasianinus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Virgibacillus.
OX   NCBI_TaxID=2017483 {ECO:0000313|EMBL:ASK63068.1, ECO:0000313|Proteomes:UP000198312};
RN   [1] {ECO:0000313|EMBL:ASK63068.1, ECO:0000313|Proteomes:UP000198312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM2416 {ECO:0000313|EMBL:ASK63068.1,
RC   ECO:0000313|Proteomes:UP000198312};
RA   Tak E.J., Bae J.-W.;
RT   "Virgibacillus sp. LM2416.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_00267}.
CC   -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000256|ARBA:ARBA00046874,
CC       ECO:0000256|HAMAP-Rule:MF_00267}.
CC   -!- SIMILARITY: Belongs to the MinC family. {ECO:0000256|ARBA:ARBA00006291,
CC       ECO:0000256|HAMAP-Rule:MF_00267}.
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DR   EMBL; CP022315; ASK63068.1; -; Genomic_DNA.
DR   RefSeq; WP_089062327.1; NZ_CP022315.1.
DR   AlphaFoldDB; A0A220U4I0; -.
DR   KEGG; vil:CFK37_13390; -.
DR   OrthoDB; 9790810at2; -.
DR   Proteomes; UP000198312; Chromosome.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:1901891; P:regulation of cell septum assembly; IEA:InterPro.
DR   Gene3D; 2.160.20.70; -; 1.
DR   Gene3D; 3.30.160.540; -; 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; IPR055219; MinC_N_1.
DR   InterPro; IPR005526; Septum_form_inhib_MinC_C.
DR   NCBIfam; TIGR01222; minC; 1.
DR   NCBIfam; NF001772; PRK00513.1-3; 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; PF22642; MinC_N_1; 1.
DR   SUPFAM; SSF63848; Cell-division inhibitor MinC, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00267};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00267}; Reference proteome {ECO:0000313|Proteomes:UP000198312};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT   DOMAIN          8..84
FT                   /note="Septum site-determining protein MinC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF22642"
FT   DOMAIN          105..205
FT                   /note="Septum formation inhibitor MinC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03775"
SQ   SEQUENCE   228 AA;  25371 MW;  D138F4ADA1F89B00 CRC64;
     MPGKKQLITI KGTRDGLTLF IDDSCSYDEA YNDLSEKLST NRPQKDEPVV SVNVQLGSRY
     LDQMQTDELK ELINNGNHFM VESIHSDVVS KKDAIQWMEE SEVKMVNQIV RSGQVVEVKG
     DLLLIGDVNP GGKVEATGNI YVMGSLLGTA HAGINGNSQA IIVASFMKPS QLRIADYISR
     APDYESDGVY MECGQIDEKQ DKIVIDRLQV LSRKQIDLNG FERRMNNG
//
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