ID A0A401ZBU5_9CHLR Unreviewed; 274 AA.
AC A0A401ZBU5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-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 ECO:0000313|EMBL:GCE04354.1};
GN ORFNames=KDAU_16830 {ECO:0000313|EMBL:GCE04354.1};
OS Dictyobacter aurantiacus.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=1936993 {ECO:0000313|EMBL:GCE04354.1, ECO:0000313|Proteomes:UP000287224};
RN [1] {ECO:0000313|Proteomes:UP000287224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-27 {ECO:0000313|Proteomes:UP000287224};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-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:GCE04354.1}.
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DR EMBL; BIFQ01000001; GCE04354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401ZBU5; -.
DR Proteomes; UP000287224; 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; 3.30.160.540; -; 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; 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:UP000287224};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 5..74
FT /note="Septum formation inhibitor MinC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05209"
FT DOMAIN 165..264
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
FT REGION 107..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 29590 MW; E13275ED7D984B14 CRC64;
MTGHIAIKGT RNGLLLTLEP ETPFSDLISA LADRLAESPA FFRGASLTVD TTHRSLRTNE
RSQLEDLLAR YHMSVSAVET VSEKRKAPKT ISLSIPDTSI EGIVTKEVGP MTKEIPPTPA
PTPSSNPPLN PSPNSSLNTK VSGPLTKDVR ETPAKDARES TDTLFIRRTV RSGQAIHHES
NVVVLGDVNP GAEIVAGGDI IVWGVLRGMV HAGYPDNENA IVCSLQLSPV QLRIAHLLSR
PPEGFEAQPR PEVATIREGQ IVVETWVSGR SPRK
//
