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Database: UniProt
Entry: A0A516KH77_9BACI
LinkDB: A0A516KH77_9BACI
Original site: A0A516KH77_9BACI 
ID   A0A516KH77_9BACI        Unreviewed;       228 AA.
AC   A0A516KH77;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   18-JUN-2025, entry version 19.
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   ECO:0000313|EMBL:QDP40744.1};
GN   ORFNames=FN924_11425 {ECO:0000313|EMBL:QDP40744.1};
OS   Radiobacillus deserti.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Radiobacillus.
OX   NCBI_TaxID=2594883 {ECO:0000313|EMBL:QDP40744.1, ECO:0000313|Proteomes:UP000315215};
RN   [1] {ECO:0000313|EMBL:QDP40744.1, ECO:0000313|Proteomes:UP000315215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKL69 {ECO:0000313|EMBL:QDP40744.1,
RC   ECO:0000313|Proteomes:UP000315215};
RA   Li J.;
RL   Submitted (JUL-2019) 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; CP041666; QDP40744.1; -; Genomic_DNA.
DR   RefSeq; WP_143894592.1; NZ_CP041666.1.
DR   AlphaFoldDB; A0A516KH77; -.
DR   KEGG; aqt:FN924_11425; -.
DR   OrthoDB; 9790810at2; -.
DR   Proteomes; UP000315215; 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:UP000315215};
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;  25680 MW;  9E193C3D9ACB0E20 CRC64;
     MIVNKQIVTI KGTRDGLTLY IDDSCSFDEM LEELEQVLSS NHVDDEEPMI TVTIQLGNRY
     LHKEQEEKLR DLIREKNRLV VQSIESNVIL KEKALEWKED SEIKIINKII RSGQVVEVKG
     DLLLIGDVNP GAKIVASGNI FVMGSLRGVA HAGAYGNQEA VIVASYMMPS QLRIADYISR
     SPDYEAEGVY MECGLIDLEK SKIVIDRLQV LSQKRPNLSG FERRMLNG
//
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