ID I4ZRZ0_9GAMM Unreviewed; 270 AA.
AC I4ZRZ0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=HADU_09141 {ECO:0000313|EMBL:EIM38982.1};
OS Acinetobacter sp. HA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1173062 {ECO:0000313|EMBL:EIM38982.1, ECO:0000313|Proteomes:UP000018434};
RN [1] {ECO:0000313|EMBL:EIM38982.1, ECO:0000313|Proteomes:UP000018434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA {ECO:0000313|EMBL:EIM38982.1,
RC ECO:0000313|Proteomes:UP000018434};
RX PubMed=22933775; DOI=10.1128/JB.01194-12;
RA Malhotra J., Dua A., Saxena A., Sangwan N., Mukherjee U., Pandey N.,
RA Rajagopal R., Khurana P., Khurana J.P., Lal R.;
RT "Genome Sequence of Acinetobacter sp. Strain HA, Isolated from the Gut of
RT the Polyphagous Insect Pest Helicoverpa armigera.";
RL J. Bacteriol. 194:5156-5156(2012).
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 -!- 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:EIM38982.1}.
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DR EMBL; AJXD01000045; EIM38982.1; -; Genomic_DNA.
DR RefSeq; WP_004811150.1; NZ_AJXD01000045.1.
DR AlphaFoldDB; I4ZRZ0; -.
DR GeneID; 58163926; -.
DR PATRIC; fig|1173062.3.peg.1789; -.
DR Proteomes; UP000018434; 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 GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 cycle {ECO:0000256|ARBA:ARBA00023210};
KW Cell division {ECO:0000313|EMBL:EIM38982.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Septation {ECO:0000256|ARBA:ARBA00023210}.
FT DOMAIN 3..166
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 270 AA; 29906 MW; E97A5B87029F1B57 CRC64;
MAKIVVVTSG KGGVGKTTTS ASFATGLALR GHKTVVIDFD VGLRNLDLIM GCERRVVYDF
VNVLNNEARL QQALIRDKDI ENLYILPASQ TRDKDALTDE GVARVMDELS QEFDYIICDS
PAGIERGAIM AMYHADEAII VTNPEISSVR DSDRIIGMLD SKTKKVEQNE GRIRKHLCIT
RFNPERADKQ EMLTIDDISK DILRVPTLGV IPECPSVLQA SNEGKPVINF TASAAGQAYD
DLVARFLGEE RPYRHIEVKP KGWLARLFGA
//
