ID A0A1V1HYX0_9FIRM Unreviewed; 265 AA.
AC A0A1V1HYX0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Septum site-determining protein MinD {ECO:0000256|ARBA:ARBA00016887};
DE AltName: Full=Cell division inhibitor MinD {ECO:0000256|ARBA:ARBA00032845};
GN ORFNames=CRIB_405 {ECO:0000313|EMBL:CED93161.1};
OS Romboutsia ilealis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=1115758 {ECO:0000313|EMBL:CED93161.1, ECO:0000313|Proteomes:UP000245622};
RN [1] {ECO:0000313|EMBL:CED93161.1, ECO:0000313|Proteomes:UP000245622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB {ECO:0000313|EMBL:CED93161.1,
RC ECO:0000313|Proteomes:UP000245622};
RA Hornung B.V.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATPase required for the correct placement of the division
CC site. Cell division inhibitors MinC and MinD act in concert to form an
CC inhibitor capable of blocking formation of the polar Z ring septums.
CC Rapidly oscillates between the poles of the cell to destabilize FtsZ
CC filaments that have formed before they mature into polar Z rings.
CC {ECO:0000256|ARBA:ARBA00025436}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC {ECO:0000256|ARBA:ARBA00010257}.
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; LN555523; CED93161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1HYX0; -.
DR Proteomes; UP000245622; Chromosome chr1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd02036; MinD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR010223; MinD.
DR InterPro; IPR025501; MinD_FleN.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01968; minD_bact; 1.
DR PANTHER; PTHR43384:SF6; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF13614; AAA_31; 1.
DR PIRSF; PIRSF003092; MinD; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000245622}.
FT DOMAIN 3..157
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 265 AA; 29175 MW; C3175E17DB77ABC9 CRC64;
MSEVIVITSG KGGVGKTTTA ANLGTALSLE NKKTVIVDAD IGLRNLDVVM GLENRIVYDI
VDVVEGTCRL KQALIKDKRF ENLYLLPAAQ TRDKNAVTVE QMSDLCNKLR ESFDYIIIDC
PAGIEQGFKN AIAGADRAIV VTNPEVSAVR DADRIIGLLE ANEINDIRLV INRIRHDMVR
RGDMMNKEDI IEILAIKLLG LVPDDESIIV STNKGEPAIL DNKSLAGQAY KNIARRILGD
EVPMLELQEE ANIFTKIKKI FGMAK
//
