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Database: UniProt
Entry: A0A256B8C2_9CYAN
LinkDB: A0A256B8C2_9CYAN
Original site: A0A256B8C2_9CYAN 
ID   A0A256B8C2_9CYAN        Unreviewed;       331 AA.
AC   A0A256B8C2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=B9G53_25950 {ECO:0000313|EMBL:OYQ61764.1};
OS   Pseudanabaena sp. SR411.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC   Pseudanabaenaceae; Pseudanabaena.
OX   NCBI_TaxID=1980935 {ECO:0000313|EMBL:OYQ61764.1, ECO:0000313|Proteomes:UP000215660};
RN   [1] {ECO:0000313|EMBL:OYQ61764.1, ECO:0000313|Proteomes:UP000215660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SR411 {ECO:0000313|EMBL:OYQ61764.1,
RC   ECO:0000313|Proteomes:UP000215660};
RA   Stowe E.L., Hundermark E.L., Stowe W.;
RT   "Novel uncharacterized cyanobacterium from Susquehanna River.";
RL   Submitted (APR-2017) 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:OYQ61764.1}.
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DR   EMBL; NDHW01000255; OYQ61764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256B8C2; -.
DR   Proteomes; UP000215660; 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   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:UP000215660};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT   DOMAIN          209..301
FT                   /note="Septum formation inhibitor MinC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03775"
FT   REGION          33..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  36091 MW;  756671227E21C1D4 CRC64;
     MPEVIVVADQ NEEYLGNVPA PLTIADVEGG ELKPIPTSLT KKSQPDPEPD PEISQVRFKT
     LDGKLNLLLP TDKKIKLPFN KSNDNGEIPP IGLDSNQFNN SETSLLTLTW EEILSQLEQR
     MAASGHDWKP RTQVYLQSGD RLLDTRQLQE LSEALQNYQL LLHCIVTNRR QTAVNAASMG
     FCVEQGTIFR ELLGFNPIPN APTDDPLYIK MTVRSGTEIR HSGSIIVFGD VNAGAELISE
     GDIIVCGKLK GMAHAGAKGN AQAVVMALHL NATQVRIASF IARVESPTTS FCPEVAFVST
     QGTPAIKIVQ VVDFSAFNHS SLNYPSLISN S
//
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