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Database: UniProt
Entry: A0A0D8CLR1_9GAMM
LinkDB: A0A0D8CLR1_9GAMM
Original site: A0A0D8CLR1_9GAMM 
ID   A0A0D8CLR1_9GAMM        Unreviewed;       250 AA.
AC   A0A0D8CLR1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=SG35_30205 {ECO:0000313|EMBL:KJE37483.1};
OS   Thalassomonas actiniarum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassomonas.
OX   NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE37483.1, ECO:0000313|Proteomes:UP000032568};
RN   [1] {ECO:0000313|EMBL:KJE37483.1, ECO:0000313|Proteomes:UP000032568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A5K-106 {ECO:0000313|EMBL:KJE37483.1,
RC   ECO:0000313|Proteomes:UP000032568};
RA   Olonade I., van Zyl L.J., Tuffin M.I.;
RT   "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT   actiniarum.";
RL   Submitted (JAN-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.
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:KJE37483.1}.
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DR   EMBL; JYNI01000093; KJE37483.1; -; Genomic_DNA.
DR   RefSeq; WP_044836226.1; NZ_CP059735.1.
DR   AlphaFoldDB; A0A0D8CLR1; -.
DR   STRING; 485447.SG35_30205; -.
DR   PATRIC; fig|485447.4.peg.6847; -.
DR   OrthoDB; 9794530at2; -.
DR   Proteomes; UP000032568; 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   CDD; cd00037; CLECT; 1.
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:UP000032568};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT   DOMAIN          6..71
FT                   /note="Septum formation inhibitor MinC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05209"
FT   DOMAIN          148..244
FT                   /note="Septum formation inhibitor MinC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03775"
FT   REGION          111..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   250 AA;  27158 MW;  502895911460D41A CRC64;
     MADATVEFKG TSFTLSVLHL KTIELSDICR DLEAKIAQAP DFFHLVPLAV NIDQVNSDSE
     IDYQAIKNLV ELLNFNFVGF TGVVAAEQKQ HIRELGLSFI NAVKTAPRKA APAKVEKTAG
     ADNAAASDKT EETPAQVPHT SVFSDKVHRG QVRSGQQLYA KDQNLVIIGS VSAGAEVIAD
     GNIHIYGALR GRAIAGAKGH HQAQIYCQNL EAELVSINGN YWLSESMEQD WGYPAYIYLT
     DTELASSKLV
//
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