MINC_AQUAE
ID MINC_AQUAE Reviewed; 201 AA.
AC O67034;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable septum site-determining protein MinC;
GN Name=minC; OrderedLocusNames=aq_878;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Cell division inhibitor that blocks the formation of polar Z
CC ring septums. Rapidly oscillates between the poles of the cell to
CC destabilize FtsZ filaments that have formed before they mature into
CC polar Z rings. Prevents FtsZ polymerization (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MinC family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06995.1; -; Genomic_DNA.
DR PIR; G70375; G70375.
DR RefSeq; NP_213596.1; NC_000918.1.
DR RefSeq; WP_010880534.1; NC_000918.1.
DR PDB; 4V02; X-ray; 2.70 A; C/D=82-201.
DR PDBsum; 4V02; -.
DR AlphaFoldDB; O67034; -.
DR SMR; O67034; -.
DR STRING; 224324.aq_878; -.
DR EnsemblBacteria; AAC06995; AAC06995; aq_878.
DR KEGG; aae:aq_878; -.
DR eggNOG; COG0850; Bacteria.
DR HOGENOM; CLU_048711_2_0_0; -.
DR InParanoid; O67034; -.
DR OMA; GHHIAIR; -.
DR OrthoDB; 1665744at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:1901891; P:regulation of cell septum assembly; IEA:InterPro.
DR Gene3D; 2.160.20.70; -; 1.
DR HAMAP; MF_00267; MinC; 1.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR013033; MinC.
DR InterPro; IPR036145; MinC_C_sf.
DR InterPro; IPR005526; Septum_form_inhib_MinC_C.
DR PANTHER; PTHR34108; PTHR34108; 1.
DR Pfam; PF03775; MinC_C; 1.
DR SUPFAM; SSF63848; SSF63848; 1.
DR TIGRFAMs; TIGR01222; minC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Reference proteome; Septation.
FT CHAIN 1..201
FT /note="Probable septum site-determining protein MinC"
FT /id="PRO_0000189012"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:4V02"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:4V02"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:4V02"
SQ SEQUENCE 201 AA; 22519 MW; A74F5613C5FADCDB CRC64;
MIEIKGKTLP VIQIKIKEKG NIDKLLKELK EKLSHNIFKG SLIILENPEV LKPEERKKVE
EILKEFSRGF IEGKKEGKEK REESRLLIIE RTLRAGQRIE HRGDILILGD VNKDAEVLAG
GNIIVMGKLR GVAKAGLIGD HSAVIVALKM EPQLLQIGKK KAIMSEADRN SPGYPEVAKI
EGEDIVLEPI EGAERWLKLL L
