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Database: UniProt
Entry: A0A0L6ZB23_9CLOT
LinkDB: A0A0L6ZB23_9CLOT
Original site: A0A0L6ZB23_9CLOT 
ID   A0A0L6ZB23_9CLOT        Unreviewed;       210 AA.
AC   A0A0L6ZB23;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:KOA20174.1};
GN   ORFNames=CLHOM_13730 {ECO:0000313|EMBL:KOA20174.1};
OS   Clostridium homopropionicum DSM 5847.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121318 {ECO:0000313|EMBL:KOA20174.1, ECO:0000313|Proteomes:UP000037043};
RN   [1] {ECO:0000313|Proteomes:UP000037043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5847 {ECO:0000313|Proteomes:UP000037043};
RA   Poehlein A., Beck M., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA   Duerre P.;
RT   "Genome sequence of the strict anaerobe Clostridium homopropionicum LuHBu1
RT   (DSM 5847T).";
RL   Submitted (AUG-2015) 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:KOA20174.1}.
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DR   EMBL; LHUR01000018; KOA20174.1; -; Genomic_DNA.
DR   RefSeq; WP_052220942.1; NZ_LHUR01000018.1.
DR   AlphaFoldDB; A0A0L6ZB23; -.
DR   STRING; 36844.SAMN04488501_111102; -.
DR   PATRIC; fig|1121318.3.peg.1383; -.
DR   Proteomes; UP000037043; 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; 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   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:UP000037043};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT   DOMAIN          103..202
FT                   /note="Septum formation inhibitor MinC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03775"
SQ   SEQUENCE   210 AA;  23802 MW;  E88D4D707244F8A7 CRC64;
     MLVDGIIIKG NREGLVAIID MNKFRDFEDM LEKLIEKLNV GKKFYKGATI KISTQLKEFN
     EKQIIILKDK LFDEFLIKGC IFEEKDEVSN KVFQGIYEGR TKFYRKTLRS GQIIRYPGNV
     VIIGDVNPGA EVYAGGNVIV LGNLQGNVYA GNSGNTKAII SAFRLYPQIL QIANIITRSP
     ENDEKPYYPE VAKIKDDTII VEPYIPNKFV
//
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