ID A0A0W0TIN0_9GAMM Unreviewed; 233 AA.
AC A0A0W0TIN0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:SPX60004.1};
GN ORFNames=Lfee_3087 {ECO:0000313|EMBL:KTC95422.1}, NCTC11978_01677
GN {ECO:0000313|EMBL:STX38493.1}, NCTC12022_00720
GN {ECO:0000313|EMBL:SPX60004.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTC95422.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTC95422.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTC95422.1,
RC ECO:0000313|Proteomes:UP000054698};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000251942, ECO:0000313|Proteomes:UP000254033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11978 {ECO:0000313|EMBL:STX38493.1,
RC ECO:0000313|Proteomes:UP000254033}, and NCTC12022
RC {ECO:0000313|EMBL:SPX60004.1, ECO:0000313|Proteomes:UP000251942};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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.
CC {ECO:0000256|ARBA:ARBA00025606, ECO:0000256|HAMAP-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|ARBA:ARBA00006291,
CC ECO:0000256|HAMAP-Rule:MF_00267}.
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DR EMBL; LNYB01000085; KTC95422.1; -; Genomic_DNA.
DR EMBL; UASS01000005; SPX60004.1; -; Genomic_DNA.
DR EMBL; UGNY01000001; STX38493.1; -; Genomic_DNA.
DR RefSeq; WP_058447880.1; NZ_UGNY01000001.1.
DR AlphaFoldDB; A0A0W0TIN0; -.
DR STRING; 453.Lfee_3087; -.
DR PATRIC; fig|453.4.peg.3368; -.
DR OrthoDB; 9794530at2; -.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR Proteomes; UP000251942; Unassembled WGS sequence.
DR Proteomes; UP000254033; 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: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 {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:UP000054698};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 11..81
FT /note="Septum formation inhibitor MinC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05209"
FT DOMAIN 134..231
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
FT REGION 111..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 233 AA; 25384 MW; 8EB4094BD44DBF31 CRC64;
MADNLLKSQA FKLKGRLYTF TVLQLLTSNR ILFEQQLHEI VTKAPRLFDR TPVVLDCSVL
AENDVDLQDL CQCMREYNLL PVAIQGANPL LTTIAQCQGL AVLHASSTHD KPLMEEPSDE
PTAVSESSKT KLQTTPVRSG QQVVSKGGDL VITASVSHGA ELLADGNIHV YGSLRGRALA
GLSGDTQARI FCQSLEAELV SIAGFYRLSD AIEPHSGPCQ IYLQDEHICI EPL
//