ID A0A257W7F5_9SPHI Unreviewed; 525 AA.
AC A0A257W7F5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE Flags: Fragment;
GN ORFNames=B7Z54_07400 {ECO:0000313|EMBL:OYW17812.1};
OS Sphingobacteriales bacterium 12-47-4.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1970580 {ECO:0000313|EMBL:OYW17812.1, ECO:0000313|Proteomes:UP000215586};
RN [1] {ECO:0000313|EMBL:OYW17812.1, ECO:0000313|Proteomes:UP000215586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-47-4 {ECO:0000313|EMBL:OYW17812.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential cell division protein that forms a contractile ring
CC structure (Z ring) at the future cell division site. The regulation of
CC the ring assembly controls the timing and the location of cell
CC division. One of the functions of the FtsZ ring is to recruit other
CC cell division proteins to the septum to produce a new cell wall between
CC the dividing cells. Binds GTP and shows GTPase activity.
CC {ECO:0000256|RuleBase:RU000631}.
CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC strictly GTP-dependent manner. {ECO:0000256|RuleBase:RU000631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000631}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000256|ARBA:ARBA00009690,
CC ECO:0000256|RuleBase:RU000631}.
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:OYW17812.1}.
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DR EMBL; NCCA01000424; OYW17812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257W7F5; -.
DR Proteomes; UP000215586; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR CDD; cd02201; FtsZ_type1; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR HAMAP; MF_00909; FtsZ; 1.
DR InterPro; IPR000158; Cell_div_FtsZ.
DR InterPro; IPR020805; Cell_div_FtsZ_CS.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR024757; FtsZ_C.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR NCBIfam; TIGR00065; ftsZ; 1.
DR PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR PANTHER; PTHR30314:SF3; MITOCHONDRIAL DIVISION PROTEIN FSZA; 1.
DR Pfam; PF12327; FtsZ_C; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU000631};
KW Cell division {ECO:0000256|RuleBase:RU000631, ECO:0000313|EMBL:OYW17812.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000631};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000631}; Septation {ECO:0000256|RuleBase:RU000631}.
FT DOMAIN 13..205
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 207..328
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 441..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 525
FT /evidence="ECO:0000313|EMBL:OYW17812.1"
SQ SEQUENCE 525 AA; 56932 MW; 185F60D53B0229CC CRC64;
MIHFDLPKEQ SSIIKVIGVG GGGSNAVNHM HNQCIDGVNF IICNTDAQAI ASSTVPNKVQ
LGPHLTQGLG AGANPEIGRQ ATEESLEEIK RILEVNTKMA FITAGMGGGT GTGGAPIISK
ICKDLGILTV GIVTTPFAYE GKKRQQQAEE GIRMLKQYVD TLLVISNDKL RHQFGNLKMR
EAFAKADNVL ATAAKCITDV ITTTGQINVD FADVCTVMKN GGVAILGSAM AEGENRAQHA
IEEALNSPLL NDNDIRGAKW ILININSAEG EHEFTMDEVE IIQNYLLSQA GEGTDVILGM
GYDSSLGSHI GITLIATGFE HKDPFDRKEV KKEEKKEEKI VMVLGQPKEE KKPEETPVVK
METRKEDPMA PKLVVEDKPV PVTSIDWTDD VVRIEETTPE VIVDERAPVV YWELNEEKKE
DSSITRETTV EKYVLASADE HLNSASRSAS SANPQQQASS VNQDKISTTP TPTSAAAGGY
LARPSNIYAE SRTEVFTSIP SAEEPVSPLP ADKKDEEEIL DLQLV
//
