ID A0A139WVT6_9CYAN Unreviewed; 376 AA.
AC A0A139WVT6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=WA1_43415 {ECO:0000313|EMBL:KYC36542.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC36542.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC36542.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC36542.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(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. {ECO:0000256|HAMAP-
CC 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|HAMAP-
CC Rule:MF_00267}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYC36542.1}.
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DR EMBL; ANNX02000047; KYC36542.1; -; Genomic_DNA.
DR RefSeq; WP_017748290.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139WVT6; -.
DR STRING; 128403.WA1_43415; -.
DR OrthoDB; 9790810at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
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; SEPTUM SITE-DETERMINING PROTEIN MINC; 1.
DR PANTHER; PTHR34108:SF1; SEPTUM SITE-DETERMINING PROTEIN MINC; 1.
DR Pfam; PF03775; MinC_C; 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:UP000076925};
KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00267}.
FT DOMAIN 258..354
FT /note="Septum formation inhibitor MinC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03775"
SQ SEQUENCE 376 AA; 41269 MW; 2125E4C83DAB0950 CRC64;
MSTYSNAEEN PIIPESEVNS VLVYLKSNSA EGNAEVISVS VSENSHSAVV KTASHFVTSE
EDSHSVVVNV ESNSVAADVE QNVAVPETES DSNLLGVESN VVPINAESKP APLIIDLNEL
PSLENTVNPN IQVQLKSEKE RLLLILPTES QVPSSEYNWT DIWQQMKLRL LACHRSFSPN
TPVYLEAQDR LLDGRQLQEL AESLGQYQVY LKSVSTSRRQ TAIAAATSGY SVEQIQPPKT
LRSEPKPTRL PLAEPLYLEK TVRSGEEVRH PGHIILLGDL NPGGIVIADG DILIWGRLRG
ITHAGANGNR ECLIMALQME PTQLRIADAV ARAPEKSPTQ YYPEVAYVTS EGIRIARSTD
FSKILLSRLS QKKDEG
//
