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Database: UniProt
Entry: E7FMS2_9LACO
LinkDB: E7FMS2_9LACO
Original site: E7FMS2_9LACO 
ID   E7FMS2_9LACO            Unreviewed;       268 AA.
AC   E7FMS2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Septum site-determining protein MinD {ECO:0000256|ARBA:ARBA00016887};
DE   AltName: Full=Cell division inhibitor MinD {ECO:0000256|ARBA:ARBA00032845};
GN   Name=minD {ECO:0000313|EMBL:EFZ35696.1};
GN   ORFNames=HMPREF0542_10199 {ECO:0000313|EMBL:EFZ35696.1};
OS   Ligilactobacillus ruminis ATCC 25644.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=525362 {ECO:0000313|EMBL:EFZ35696.1, ECO:0000313|Proteomes:UP000004099};
RN   [1] {ECO:0000313|EMBL:EFZ35696.1, ECO:0000313|Proteomes:UP000004099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25644 {ECO:0000313|EMBL:EFZ35696.1,
RC   ECO:0000313|Proteomes:UP000004099};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) 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   -!- 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:EFZ35696.1}.
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DR   EMBL; ACGS02000014; EFZ35696.1; -; Genomic_DNA.
DR   RefSeq; WP_003694397.1; NZ_GL833109.1.
DR   AlphaFoldDB; E7FMS2; -.
DR   PATRIC; fig|525362.12.peg.250; -.
DR   HOGENOM; CLU_037612_0_1_9; -.
DR   Proteomes; UP000004099; Unassembled WGS sequence.
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}.
FT   DOMAIN          3..157
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
SQ   SEQUENCE   268 AA;  29195 MW;  E8CCA70833E33789 CRC64;
     MGRAIVITSG KGGVGKTTTT ANLGSALALM GKKVIMLDLD IGLRNLDVVL GLDNRIIYDI
     VDVAKGRCKL HQAIIKDKRF EDKLFLLPAA QNTDKSAIEP EEVKAIVADL KSDFDYILLD
     CPAGIEQGFA NSVAGADEAI VVSTPEISAV RDADRVVGLL EQADLDEPPM LIINRIKKRM
     VNDGTMMDVD EITHHLSIKL IGIVFDDDEV IGTSNKGEPI VLNEKSPASK GYRNIARRLE
     GQTVPLMTMK ESDESGFFGK IASWFQKK
//
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