MIND_NEIMB
ID MIND_NEIMB Reviewed; 271 AA.
AC Q7DDS7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Septum site-determining protein MinD;
DE AltName: Full=Cell division inhibitor MinD;
GN Name=minD; OrderedLocusNames=NMB0171;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=NZ98/254 / Serogroup B;
RX PubMed=16645985; DOI=10.1002/pmic.200500821;
RA Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT prepared from the group B strain NZ98/254.";
RL Proteomics 6:3400-3413(2006).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MinC and FtsZ. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC used as vaccines in human.
CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily. {ECO:0000305}.
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DR EMBL; AE002098; AAF40628.1; -; Genomic_DNA.
DR PIR; C81230; C81230.
DR RefSeq; NP_273229.1; NC_003112.2.
DR RefSeq; WP_002215463.1; NC_003112.2.
DR AlphaFoldDB; Q7DDS7; -.
DR SMR; Q7DDS7; -.
DR STRING; 122586.NMB0171; -.
DR PaxDb; Q7DDS7; -.
DR PRIDE; Q7DDS7; -.
DR EnsemblBacteria; AAF40628; AAF40628; NMB0171.
DR GeneID; 61282240; -.
DR KEGG; nme:NMB0171; -.
DR PATRIC; fig|122586.8.peg.212; -.
DR HOGENOM; CLU_037612_0_1_4; -.
DR OMA; CESAKAY; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0051782; P:negative regulation of cell division; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR010223; MinD.
DR InterPro; IPR025501; MinD_FleN.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01656; CbiA; 1.
DR PIRSF; PIRSF003092; MinD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01968; minD_bact; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW Membrane; Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..271
FT /note="Septum site-determining protein MinD"
FT /id="PRO_0000320272"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q72H90"
SQ SEQUENCE 271 AA; 29559 MW; 9ACDB52A03BD6170 CRC64;
MAKIIVVTSG KGGVGKTTTS ASIATGLALR GYKTAVIDFD VGLRNLDLIM GCERRVVYDL
INVIQGEATL NQALIKDKNC ENLFILPASQ TRDKDALTRE GVEKVMQELS GKKMGFEYII
CDSPAGIEQG ALMALYFADE AIVTTNPEVS SVRDSDRILG ILQSKSHKAE QGGSVKEHLL
ITRYSPERVA KGEMLSVQDI CDILHIPLLG VIPESQNVLQ ASNSGEPVIH QDSVAASEAY
KDVIARLLGE NREMRFLEAE KKSFFKRLFG G