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Database: UniProt
Entry: A0A1J0PB65_9SYNE
LinkDB: A0A1J0PB65_9SYNE
Original site: A0A1J0PB65_9SYNE 
ID   A0A1J0PB65_9SYNE        Unreviewed;       242 AA.
AC   A0A1J0PB65;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=BM449_09150 {ECO:0000313|EMBL:APD48380.1};
OS   Synechococcus sp. SynAce01.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1916956 {ECO:0000313|EMBL:APD48380.1, ECO:0000313|Proteomes:UP000182608};
RN   [1] {ECO:0000313|Proteomes:UP000182608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SynAce01 {ECO:0000313|Proteomes:UP000182608};
RA   Tang J., Daroch M., Liang Y., Jiang D., Shah M.;
RL   Submitted (NOV-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}.
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DR   EMBL; CP018091; APD48380.1; -; Genomic_DNA.
DR   RefSeq; WP_071801016.1; NZ_CP018091.1.
DR   AlphaFoldDB; A0A1J0PB65; -.
DR   STRING; 1916956.BM449_09150; -.
DR   KEGG; syny:BM449_09150; -.
DR   OrthoDB; 9790810at2; -.
DR   Proteomes; UP000182608; Chromosome.
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:UP000182608};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT   DOMAIN          132..223
FT                   /note="Septum formation inhibitor MinC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03775"
FT   REGION          99..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   242 AA;  25183 MW;  F8015BD4522D8D47 CRC64;
     MAALFLAAAR PGLSHHLLLP EWTRQSGAVD DVLRHDLEQH SPPGGAVILH ANHWRLTLPE
     LQALRQRLQR QGLTLIGVEC RNTETLVAAA ALGVTASAGA DLTPTTPPVA TASSSPAEPS
     PQPVIPPDPL TIHRGTLRSG DHLQVEGSLL VLGDVNPGAR ASAAGHVLVW GRLRGIAHAG
     CLGDGSARIV ALELRPLQLR IAAAVARGPS DPPPAGLSEE ARLVDGVIRI DPAQATWPLG
     LA
//
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