ID A0A7X0HU07_9BACI Unreviewed; 228 AA.
AC A0A7X0HU07;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 18-JUN-2025, entry version 14.
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=HNR53_002526 {ECO:0000313|EMBL:MBB6445877.1};
OS Bacillus benzoevorans.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1456 {ECO:0000313|EMBL:MBB6445877.1, ECO:0000313|Proteomes:UP000531594};
RN [1] {ECO:0000313|EMBL:MBB6445877.1, ECO:0000313|Proteomes:UP000531594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5391 {ECO:0000313|EMBL:MBB6445877.1,
RC ECO:0000313|Proteomes:UP000531594};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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}.
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:MBB6445877.1}.
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DR EMBL; JACHGK010000008; MBB6445877.1; -; Genomic_DNA.
DR RefSeq; WP_184526334.1; NZ_JACHGK010000008.1.
DR AlphaFoldDB; A0A7X0HU07; -.
DR Proteomes; UP000531594; 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 NCBIfam; TIGR01222; minC; 1.
DR NCBIfam; NF001772; PRK00513.1-3; 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; 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:UP000531594};
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 107..208
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
SQ SEQUENCE 228 AA; 25508 MW; 9FFC9C27E1474106 CRC64;
MIKNQNVTIK GTKDGLTLHL DHLCSYDELK RELQMKLSET ARTQEVNQLI NVKVQAGYRF
LSEEQKEEIL EIIKQKKNFI VNGIDSNVMT IEEVTKMKQE QEVVSLSKIV RSGQVIQVPG
DLLLIGDVNP GGTVMAGGNI YVMGALRGIA HAGCNGNKQA VIAAAVMMPS QLRIADYINR
APDPDYTKEQ EKREMECAYI DENNQIIIDR LQVLMQLRPN LTKLEGGL
//
