MINC_BORA1
ID MINC_BORA1 Reviewed; 278 AA.
AC Q2KVW8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Probable septum site-determining protein MinC {ECO:0000255|HAMAP-Rule:MF_00267};
GN Name=minC {ECO:0000255|HAMAP-Rule:MF_00267}; OrderedLocusNames=BAV2788;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00267}.
CC -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000255|HAMAP-
CC Rule:MF_00267}.
CC -!- SIMILARITY: Belongs to the MinC family. {ECO:0000255|HAMAP-
CC Rule:MF_00267}.
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DR EMBL; AM167904; CAJ50399.1; -; Genomic_DNA.
DR RefSeq; WP_012418430.1; NC_010645.1.
DR AlphaFoldDB; Q2KVW8; -.
DR SMR; Q2KVW8; -.
DR STRING; 360910.BAV2788; -.
DR EnsemblBacteria; CAJ50399; CAJ50399; BAV2788.
DR GeneID; 41394625; -.
DR KEGG; bav:BAV2788; -.
DR eggNOG; COG0850; Bacteria.
DR HOGENOM; CLU_067812_0_0_4; -.
DR OMA; RRDPLWG; -.
DR OrthoDB; 1665744at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0051302; P:regulation of cell division; IEA:InterPro.
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; IPR007874; MinC_N.
DR InterPro; IPR005526; Septum_form_inhib_MinC_C.
DR PANTHER; PTHR34108; PTHR34108; 1.
DR Pfam; PF03775; MinC_C; 1.
DR Pfam; PF05209; MinC_N; 1.
DR SUPFAM; SSF63848; SSF63848; 1.
DR TIGRFAMs; TIGR01222; minC; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Reference proteome; Septation.
FT CHAIN 1..278
FT /note="Probable septum site-determining protein MinC"
FT /id="PRO_1000047805"
FT REGION 104..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 29374 MW; 78478097B568B77A CRC64;
MTTEPLALDF KSATLYAIRV VLHSADPDQL AEALGRRMAD AGSFFENEAV VIDASRVSAP
IDWPALVKAL GAHKLPVIGV VAENGNLERA RAAGLIPVEL SAPRTQQSVD PAPPNHVSTP
VPAAPEASRA AQEQLRSAMK GDAQAVPTRA ARDTTEAASH TPAAPQSSTA LVITKPLRSG
QRVYARHTDL VVIGMVSQGA EVIADGNIHV YGPLRGKAMA GARGDTSARI FTTHLDAELL
AVAGVYRVVE DRLDRNLHNQ PALVRLNGDT LHIEALKS