ID A0A2Z6ETT5_9BURK Unreviewed; 244 AA.
AC A0A2Z6ETT5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=MCB1EB_0678 {ECO:0000313|EMBL:BBE08839.1};
OS Mycoavidus cysteinexigens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Mycoavidus.
OX NCBI_TaxID=1553431 {ECO:0000313|EMBL:BBE08839.1, ECO:0000313|Proteomes:UP000282597};
RN [1] {ECO:0000313|EMBL:BBE08839.1, ECO:0000313|Proteomes:UP000282597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1-EB {ECO:0000313|EMBL:BBE08839.1,
RC ECO:0000313|Proteomes:UP000282597};
RX PubMed=29540638; DOI=10.1264/jsme2.ME17138;
RA Sharmin D., Guo Y., Nishizawa T., Ohshima S., Sato Y., Takashima Y.,
RA Narisawa K., Ohta H.;
RT "Comparative Genomic Insights into Endofungal Lifestyles of Two Bacterial
RT Endosymbionts, Mycoavidus cysteinexigens and Burkholderia rhizoxinica.";
RL Microbes Environ. 33:66-76(2018).
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; AP018150; BBE08839.1; -; Genomic_DNA.
DR RefSeq; WP_045362958.1; NZ_BSOD01000012.1.
DR AlphaFoldDB; A0A2Z6ETT5; -.
DR KEGG; mcys:MCB1EB_0678; -.
DR Proteomes; UP000282597; 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:UP000282597};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 9..80
FT /note="Septum formation inhibitor MinC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05209"
FT DOMAIN 138..239
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
SQ SEQUENCE 244 AA; 26767 MW; 7DA831234BD4DA8F CRC64;
MSNKKTSCFE LRSSSFDTLL FTVKTADLEV LHQTLKRRFE VAPEFFANDI VVIDVRPLHP
DETIEIDALA AMLREVRMYP VGIAAHEAQR VWAQQSDLPF VEAGVGRIPP SAAHATNPVT
PPTPKLEQPI EDYKSALVID KPLRSGQQVY AKGDLIVLGV VSYGAEVIAE GHIHIYAPLR
GRALAGAQGN LNARIFCTCL EPELLSIAGI YRTTETPLPA QVQGKPVQVS LLNEKLVIEP
LKLT
//