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Database: UniProt
Entry: A0A1R1MKD7_9BACT
LinkDB: A0A1R1MKD7_9BACT
Original site: A0A1R1MKD7_9BACT 
ID   A0A1R1MKD7_9BACT        Unreviewed;       218 AA.
AC   A0A1R1MKD7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=BLW93_06220 {ECO:0000313|EMBL:OMH40278.1};
OS   Desulfurobacterium indicum.
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Desulfurobacterium.
OX   NCBI_TaxID=1914305 {ECO:0000313|EMBL:OMH40278.1, ECO:0000313|Proteomes:UP000187408};
RN   [1] {ECO:0000313|EMBL:OMH40278.1, ECO:0000313|Proteomes:UP000187408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K6013 {ECO:0000313|EMBL:OMH40278.1,
RC   ECO:0000313|Proteomes:UP000187408};
RA   Cao J., Shao Z., Alain K., Jebbar M.;
RT   "Genome sequence of a sulfur-reducing bacterium Desulfurobacterium indicum
RT   K6013.";
RL   Submitted (OCT-2016) 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|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:OMH40278.1}.
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DR   EMBL; MOEN01000022; OMH40278.1; -; Genomic_DNA.
DR   RefSeq; WP_076713241.1; NZ_MOEN01000022.1.
DR   AlphaFoldDB; A0A1R1MKD7; -.
DR   STRING; 1914305.BLW93_06220; -.
DR   OrthoDB; 9790810at2; -.
DR   Proteomes; UP000187408; 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   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:UP000187408};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT   DOMAIN          114..185
FT                   /note="Septum formation inhibitor MinC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03775"
SQ   SEQUENCE   218 AA;  24719 MW;  29CE64D22BDAA809 CRC64;
     MDYKIRGTNI LGIEVIVSNS NLNIEKLKNF LLEKKAILKR TRLIITFDNI IPDENEIREI
     ASFCSELPDV FFCGFKTNKK ETRDNCISAG FPCDMSKLEL EKKSERASTE EIKFVKKTVR
     SGEKVSSSGD IAILGDVNPG AEVEAGGNVY IFGSLRGLVK AGIGKKECEV RALFVQTPRI
     EVCGREKTFE RKEKFFNFRL IYKNDKIRIF TTERVDNG
//
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