ID A0A4Q2IXE0_9BURK Unreviewed; 255 AA.
AC A0A4Q2IXE0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 13.
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:RXZ33890.1};
GN ORFNames=D9O50_12430 {ECO:0000313|EMBL:RXZ33890.1};
OS Oxalobacteraceae bacterium CAVE-383.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Oxalobacteraceae.
OX NCBI_TaxID=2478672 {ECO:0000313|EMBL:RXZ33890.1, ECO:0000313|Proteomes:UP000289999};
RN [1] {ECO:0000313|EMBL:RXZ33890.1, ECO:0000313|Proteomes:UP000289999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAVE-383 {ECO:0000313|EMBL:RXZ33890.1,
RC ECO:0000313|Proteomes:UP000289999};
RA Coelho C., Verissimo A., Tiago I.;
RT "Draft Genome Sequence of Pseudoherbaspirillum foraminis sp. nov., a
RT bacterium isolated from a karstic cave dripping water in Portugal.";
RL Submitted (OCT-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}.
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:RXZ33890.1}.
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DR EMBL; REGP01000003; RXZ33890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q2IXE0; -.
DR OrthoDB; 9794530at2; -.
DR Proteomes; UP000289999; 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:UP000289999};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 8..78
FT /note="Septum formation inhibitor MinC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05209"
FT DOMAIN 148..247
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
FT REGION 105..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..144
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 255 AA; 26771 MW; D6CC54CC92548EF3 CRC64;
MQKNRKPIEI KISTVVAISA LLHESAPAEI DKALREMTGG ASDFFEDEFA VLDIASLPAG
AEIDWPALIA VFKTYRLNAV AVRHAPPEMH AGIVAHGLSI ADGAVKAPPA EPEAAESRPA
APARATAAAP APATAPPQQQ TQTQSTMIID TPVRAGTRIY ARGADLVVMA AVNNGAEIIA
DGSIHVYAPL RGRALAGASG NADARIFTTS MEAELISIAG VYRTFEKDLP PELANKPVQV
RLSGDRLDML AIKNT
//
