GenomeNet

Database: UniProt
Entry: W8T6D8_PEPAC
LinkDB: W8T6D8_PEPAC
Original site: W8T6D8_PEPAC 
ID   W8T6D8_PEPAC            Unreviewed;       203 AA.
AC   W8T6D8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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:AHM56450.1};
GN   ORFNames=EAL2_c11540 {ECO:0000313|EMBL:AHM56450.1};
OS   Peptoclostridium acidaminophilum DSM 3953.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1286171 {ECO:0000313|EMBL:AHM56450.1, ECO:0000313|Proteomes:UP000019591};
RN   [1] {ECO:0000313|EMBL:AHM56450.1, ECO:0000313|Proteomes:UP000019591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3953 {ECO:0000313|EMBL:AHM56450.1,
RC   ECO:0000313|Proteomes:UP000019591};
RX   PubMed=24926057;
RA   Poehlein A., Andreesen J.R., Daniel R.;
RT   "Complete Genome Sequence of Amino Acid-Utilizing Eubacterium
RT   acidaminophilum al-2 (DSM 3953).";
RL   Genome Announc. 2:e00573-14(2014).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP007452; AHM56450.1; -; Genomic_DNA.
DR   RefSeq; WP_025435454.1; NZ_CP007452.1.
DR   AlphaFoldDB; W8T6D8; -.
DR   STRING; 1286171.EAL2_c11540; -.
DR   KEGG; eac:EAL2_c11540; -.
DR   PATRIC; fig|1286171.3.peg.1102; -.
DR   eggNOG; COG0850; Bacteria.
DR   HOGENOM; CLU_048711_2_0_9; -.
DR   OrthoDB; 9790810at2; -.
DR   Proteomes; UP000019591; 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   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:UP000019591};
KW   Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT   DOMAIN          96..197
FT                   /note="Septum formation inhibitor MinC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03775"
SQ   SEQUENCE   203 AA;  22224 MW;  C0469E0E7F78D132 CRC64;
     MLETEKVEFK GTKNGLVINI GNDCDYKTAR ELIGSKVKGA NGFFDGARIY AINCGGVDDV
     EYIMLKEYIE SELGMQIAEE ERQLAIEYVS SGDTKFIRST LRSGKRVEFS GNIVIIGDVN
     PGAHIVADGN VVVIGALRGV VHAGAGGNRE AFVVANNLEP MQLRIAESIA IPPEEEHEDK
     PDIPEIAFIK ENYIIIEPCL NRK
//
DBGET integrated database retrieval system