ID A0A3N9UKN1_9BACI Unreviewed; 222 AA.
AC A0A3N9UKN1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=EBB45_02565 {ECO:0000313|EMBL:RQW76451.1};
OS Lysinibacillus composti.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=720633 {ECO:0000313|EMBL:RQW76451.1, ECO:0000313|Proteomes:UP000274033};
RN [1] {ECO:0000313|EMBL:RQW76451.1, ECO:0000313|Proteomes:UP000274033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A12701 {ECO:0000313|EMBL:RQW76451.1,
RC ECO:0000313|Proteomes:UP000274033};
RX PubMed=23812821; DOI=10.1007/s12275-013-2664-1;
RA Kim S.J., Jang Y.H., Hamada M., Ahn J.H., Weon H.Y., Suzuki K., Whang K.S.,
RA Kwon S.W.;
RT "Lysinibacillus chungkukjangi sp. nov., isolated from Chungkukjang, Korean
RT fermented soybean food.";
RL J. Microbiol. 51:400-404(2013).
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|HAMAP-
CC Rule:MF_00267}.
CC -!- SIMILARITY: Belongs to the MinC family. {ECO:0000256|HAMAP-
CC Rule:MF_00267}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQW76451.1}.
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DR EMBL; RRCT01000001; RQW76451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N9UKN1; -.
DR OrthoDB; 9790810at2; -.
DR Proteomes; UP000274033; 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; 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 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:UP000274033};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 103..193
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
SQ SEQUENCE 222 AA; 24543 MW; 7B6A18762B0824A4 CRC64;
MKKQLVHIKG TKEGLVLRLD DQCAYAELVE ELERKVSEGG IDSKVDVQLY LGYRYCTSEQ
MTELIQIVQG PGKMLVSNVH SEVITVEECN HRMLENQCDT YVGIVRSGQV LKAEGDIIVI
GDVNPNGRIE AGGNIYILGN LKGMVHAGVN GKEDVIIAAS HFLPTHVMIA DQIEVMSNEQ
PIVLKNADQL FAYINSDGKI SYNRLQDFRN IRPLLTTSKG GS
//
