ID A0A1S8CPK5_9GAMM Unreviewed; 270 AA.
AC A0A1S8CPK5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BMI79_02595 {ECO:0000313|EMBL:OMQ27235.1};
OS Serratia oryzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=2034155 {ECO:0000313|EMBL:OMQ27235.1, ECO:0000313|Proteomes:UP000216021};
RN [1] {ECO:0000313|EMBL:OMQ27235.1, ECO:0000313|Proteomes:UP000216021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J11-6 {ECO:0000313|EMBL:OMQ27235.1,
RC ECO:0000313|Proteomes:UP000216021};
RA Zhang X.-X., Zhang J.;
RT "Rahnella oryzae sp. nov., isolated from rice root.";
RL Submitted (NOV-2016) 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 -!- SUBUNIT: Interacts with MinC and FtsZ. {ECO:0000256|ARBA:ARBA00011626}.
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:OMQ27235.1}.
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DR EMBL; MOXD01000001; OMQ27235.1; -; Genomic_DNA.
DR RefSeq; WP_076940271.1; NZ_SOZF01000018.1.
DR AlphaFoldDB; A0A1S8CPK5; -.
DR STRING; 2034155.BMI79_02595; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000216021; Unassembled WGS sequence.
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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_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; PF01656; CbiA; 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 cycle {ECO:0000256|ARBA:ARBA00023210};
KW Cell division {ECO:0000256|ARBA:ARBA00023210};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Septation {ECO:0000256|ARBA:ARBA00023210}.
FT DOMAIN 5..227
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 270 AA; 29640 MW; 21DC7FAD884888E4 CRC64;
MARIIVVTSG KGGVGKTTSS AAIATGLAQK GKKTVVIDFD IGLRNLDLIM GCERRVVYDF
VNVIQGDATL NQALIKDKRT ENLYILPASQ TRDKDALTRE GVEKILNDLD EMGFEFVVCD
SPAGIETGAL MALYFADEAI ITTNPEVSSV RDSDRILGIL ASKSRRAEKG EAPIQEHLLL
TRYNPGRVSR GDMLSMEDVL EILRIPLVGV IPEDQSVLRA SNQGEPVILD SESDAGKAYD
DTVHRLLGEE RPFRFIEEEK KGFLKRLFGG
//
