ID E0IDV0_9BACL Unreviewed; 221 AA.
AC E0IDV0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 18-JUN-2025, entry version 54.
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=PaecuDRAFT_3841 {ECO:0000313|EMBL:EFM09304.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM09304.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM09304.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM09304.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) 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; AEDD01000011; EFM09304.1; -; Genomic_DNA.
DR RefSeq; WP_006039827.1; NZ_AEDD01000011.1.
DR AlphaFoldDB; E0IDV0; -.
DR STRING; 717606.PaecuDRAFT_3841; -.
DR eggNOG; COG0850; Bacteria.
DR Proteomes; UP000005387; Unassembled WGS sequence.
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 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:UP000005387};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 7..84
FT /note="Septum site-determining protein MinC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF22642"
FT DOMAIN 104..197
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
SQ SEQUENCE 221 AA; 24391 MW; A4D265492EEC33A0 CRC64;
MTEKQHITIK GVKEGLVFLL DDRCEFSALL DELHYKLEKT HQQLLSGPLI HVHVKLGSRE
TTEDEKDRIK SVLRQRGNLL VQSIQSEAEQ VSAANSNKQE MKVMSGIIRS GQVVTHDGSL
LLLGDLHPGG SIICTGDIYV MGTLAGMAHA GAEGNADAII ASSLLRPTQL RIAEVISRPP
EEWMTGDAAM EYAFLQEGIM QVDKTTQLFR MRKDPIVYKG V
//