ID A0A1Q2SPZ1_9GAMM Unreviewed; 247 AA.
AC A0A1Q2SPZ1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Probable septum site-determining protein MinC {ECO:0000256|HAMAP-Rule:MF_00267};
GN Name=minC {ECO:0000256|HAMAP-Rule:MF_00267};
GN ORFNames=TAO_1811 {ECO:0000313|EMBL:BAW81181.1};
OS Candidatus Nitrosoglobus terrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Candidatus Nitrosoglobus.
OX NCBI_TaxID=1630141 {ECO:0000313|EMBL:BAW81181.1, ECO:0000313|Proteomes:UP000243679};
RN [1] {ECO:0000313|EMBL:BAW81181.1, ECO:0000313|Proteomes:UP000243679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAO100 {ECO:0000313|EMBL:BAW81181.1,
RC ECO:0000313|Proteomes:UP000243679};
RX PubMed=28072419; DOI=10.1038/ismej.2016.191;
RA Hayatsu M., Tago K., Uchiyama I., Toyoda A., Wang Y., Shimomura Y.,
RA Okubo T., Kurisu F., Hirono Y., Nonaka K., Akiyama H., Itoh T., Takami H.;
RT "An acid-tolerant ammonia-oxidizing ?-proteobacterium from soil.";
RL ISME J. 11:1130-1141(2017).
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.
CC {ECO:0000256|ARBA:ARBA00025606, ECO:0000256|HAMAP-Rule:MF_00267}.
CC -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000256|HAMAP-
CC Rule:MF_00267}.
CC -!- SIMILARITY: Belongs to the MinC family. {ECO:0000256|ARBA:ARBA00006291,
CC ECO:0000256|HAMAP-Rule:MF_00267}.
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DR EMBL; AP014836; BAW81181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2SPZ1; -.
DR KEGG; ntt:TAO_1811; -.
DR OrthoDB; 9794530at2; -.
DR Proteomes; UP000243679; 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 Gene3D; 3.30.70.260; -; 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 NCBIfam; TIGR01222; minC; 1.
DR PANTHER; PTHR34108; SEPTUM SITE-DETERMINING PROTEIN MINC; 1.
DR PANTHER; PTHR34108:SF1; SEPTUM SITE-DETERMINING PROTEIN MINC; 1.
DR Pfam; PF03775; MinC_C; 1.
DR Pfam; PF05209; MinC_N; 1.
DR SUPFAM; SSF63848; Cell-division inhibitor MinC, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00267};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00267}; Reference proteome {ECO:0000313|Proteomes:UP000243679};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 12..84
FT /note="Septum formation inhibitor MinC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05209"
FT DOMAIN 144..244
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
SQ SEQUENCE 247 AA; 27278 MW; 3797A4DB14F6F1E8 CRC64;
MPPLAFNSKR AFELKGELFT LSVLQLQDTD IEHITHELIA KIRTAPGFFS STPIIIDLKN
LNNRESLIDF NALKAVLIEH GLVPVGVRNA RSKNQIAAAQ AGLALLRSEP IEDTFSEKQN
NAKHQPFQIN IDHTDPYSPH KSIIITRPVR SGQQIYAQNC DLILLAQASP GSELLADGSI
HIYGPLRGRA LAGIHGDRKV RIFCQSLEAE LIAIAGNYKV INDIEPTLKS RPVQIYLQGD
HLMVSAL
//