ID A0A494Z5W7_9BACI Unreviewed; 228 AA.
AC A0A494Z5W7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 10.
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:RKQ17939.1};
GN ORFNames=D8M05_03360 {ECO:0000313|EMBL:RKQ17939.1};
OS Oceanobacillus bengalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=1435466 {ECO:0000313|EMBL:RKQ17939.1, ECO:0000313|Proteomes:UP000281813};
RN [1] {ECO:0000313|EMBL:RKQ17939.1, ECO:0000313|Proteomes:UP000281813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1K00260 {ECO:0000313|EMBL:RKQ17939.1,
RC ECO:0000313|Proteomes:UP000281813};
RX PubMed=26303283; DOI=10.1007/s10482-015-0573-5;
RA Yongchang O., Xiang W., Wang G.;
RT "Oceanobacillus bengalensis sp. nov., a bacterium isolated from seawater of
RT the Bay of Bengal.";
RL Antonie Van Leeuwenhoek 108:1189-1196(2015).
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:RKQ17939.1}.
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DR EMBL; RBZO01000003; RKQ17939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494Z5W7; -.
DR OrthoDB; 9790810at2; -.
DR Proteomes; UP000281813; 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:UP000281813};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 106..205
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
SQ SEQUENCE 228 AA; 26119 MW; 6F39E1D4B7F75099 CRC64;
MHDTKQLITI KGTREGITLF IDESCSFNQA MNELHDKIIS SRPKNDEPIV SVKVKLGNRY
LKEEQEKDLR KIFNEENRFE IHSIESDVIR KEDALKWIEE SKMKLVNRIV RSGQVLEIDG
DLLLIGDVNP GGKVVSTGNI FIMGHLYGIA HAGVDGDRSA FIVASYMKPT QLRIADYLSR
APDYESDGVY MECGLIDEEQ DKIIIDRLQV LSHKRKEISR FERRIQNG
//
