ID M4XJA4_9PSED Unreviewed; 304 AA.
AC M4XJA4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 66.
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 ECO:0000313|EMBL:AGI25355.1};
GN ORFNames=H681_17435 {ECO:0000313|EMBL:AGI25355.1};
OS Pseudomonas sp. ATCC 13867.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI25355.1, ECO:0000313|Proteomes:UP000012082};
RN [1] {ECO:0000313|EMBL:AGI25355.1, ECO:0000313|Proteomes:UP000012082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI25355.1,
RC ECO:0000313|Proteomes:UP000012082};
RX PubMed=23723394;
RA Ainala S.K., Somasundar A., Park S.;
RT "Complete genome sequence of Pseudomonas denitrificans ATCC 13867.";
RL Genome Announc. 1:E00257-E00213(2013).
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; CP004143; AGI25355.1; -; Genomic_DNA.
DR RefSeq; WP_015478208.1; NC_020829.1.
DR AlphaFoldDB; M4XJA4; -.
DR STRING; 1294143.H681_17435; -.
DR KEGG; pdr:H681_17435; -.
DR PATRIC; fig|1294143.3.peg.3537; -.
DR eggNOG; COG0850; Bacteria.
DR HOGENOM; CLU_067812_0_0_6; -.
DR OrthoDB; 9794530at2; -.
DR Proteomes; UP000012082; 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};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 13..84
FT /note="Septum formation inhibitor MinC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05209"
FT DOMAIN 201..301
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
SQ SEQUENCE 304 AA; 32547 MW; A61900E41EEB83B9 CRC64;
MSQADLLDHD PVFQLKGSML AVTVLELAHN DLPRLDRQLA DKVAQAPNFF RDTPLVLALD
KLPDGEGQLD LQGVLDICRR HGLRTLAIRA SREEDIRLAT MFDIPVLPPS GSSRERTVEP
KDPATPLTGA TPVRRPRSER LSEKVVEQAA GGATVQPENS TGKATEIQAE KSAETQEPIT
DATPEKPAEP PAPVVRPTKL VTSPVRGGVQ IYAAGGDLIV LAPVSPGAEL LADGNIHVYG
PMRGRALAGV KGDTSARIFC QQLAAELVSI AGNYKVAEDL RRSPQWGQAV HVSLSGDVLN
ITRL
//