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MINE_NEIGO
ID   MINE_NEIGO              Reviewed;          87 AA.
AC   P58152;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cell division topological specificity factor;
GN   Name=minE;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CH811;
RX   PubMed=11160816; DOI=10.1099/00221287-147-1-225;
RA   Ramirez-Arcos S., Szeto J., Beveridge T., Victor C., Francis F., Dillon J.;
RT   "Deletion of the cell-division inhibitor MinC results in lysis of Neisseria
RT   gonorrhoeae.";
RL   Microbiology 147:225-237(2001).
CC   -!- FUNCTION: Prevents the cell division inhibition by proteins MinC and
CC       MinD at internal division sites while permitting inhibition at polar
CC       sites. This ensures cell division at the proper site by restricting the
CC       formation of a division septum at the midpoint of the long axis of the
CC       cell (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P58152; Q9AG19: minD; NbExp=2; IntAct=EBI-15883835, EBI-15883863;
CC       P58152; P58152: minE; NbExp=2; IntAct=EBI-15883835, EBI-15883835;
CC   -!- SIMILARITY: Belongs to the MinE family. {ECO:0000305}.
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DR   EMBL; AF345908; AAK30127.1; -; Genomic_DNA.
DR   RefSeq; WP_003690052.1; NZ_WHPL01000002.1.
DR   PDB; 2KXO; NMR; -; A/B=1-87.
DR   PDB; 6U6P; NMR; -; A/B=1-81.
DR   PDB; 6U6Q; NMR; -; A/B=11-87.
DR   PDB; 6U6R; NMR; -; A/B=31-87.
DR   PDB; 6U6S; NMR; -; A/B=11-87.
DR   PDBsum; 2KXO; -.
DR   PDBsum; 6U6P; -.
DR   PDBsum; 6U6Q; -.
DR   PDBsum; 6U6R; -.
DR   PDBsum; 6U6S; -.
DR   AlphaFoldDB; P58152; -.
DR   BMRB; P58152; -.
DR   SMR; P58152; -.
DR   DIP; DIP-59460N; -.
DR   IntAct; P58152; 1.
DR   PRIDE; P58152; -.
DR   GeneID; 66754325; -.
DR   EvolutionaryTrace; P58152; -.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0032955; P:regulation of division septum assembly; IEA:InterPro.
DR   Gene3D; 3.30.1070.10; -; 1.
DR   HAMAP; MF_00262; MinE; 1.
DR   InterPro; IPR005527; MinE.
DR   InterPro; IPR036707; MinE_sf.
DR   Pfam; PF03776; MinE; 1.
DR   SUPFAM; SSF55229; SSF55229; 1.
DR   TIGRFAMs; TIGR01215; minE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division.
FT   CHAIN           1..87
FT                   /note="Cell division topological specificity factor"
FT                   /id="PRO_0000205879"
FT   HELIX           3..7
FT                   /evidence="ECO:0007829|PDB:2KXO"
FT   STRAND          18..30
FT                   /evidence="ECO:0007829|PDB:2KXO"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:6U6Q"
FT   HELIX           40..54
FT                   /evidence="ECO:0007829|PDB:2KXO"
FT   STRAND          61..69
FT                   /evidence="ECO:0007829|PDB:2KXO"
FT   STRAND          72..81
FT                   /evidence="ECO:0007829|PDB:2KXO"
SQ   SEQUENCE   87 AA;  10041 MW;  AF5A261D415FE7C3 CRC64;
     MSLIELLFGR KQKTATVARD RLQIIIAQER AQEGQTPDYL PTLRKELMEV LSKYVNVSLD
     NIRISQEKQD GMDVLELNIT LPEQKKV
 
 
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