ID A0A1S1J257_9FLAO Unreviewed; 675 AA.
AC A0A1S1J257;
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=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631};
GN Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909};
GN ORFNames=BHE19_18650 {ECO:0000313|EMBL:OHT43316.1};
OS Flavobacterium tructae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1114873 {ECO:0000313|EMBL:OHT43316.1, ECO:0000313|Proteomes:UP000180252};
RN [1] {ECO:0000313|Proteomes:UP000180252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSU {ECO:0000313|Proteomes:UP000180252};
RA Chen S., Walker E.;
RL Submitted (SEP-2016) 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|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC strictly GTP-dependent manner. Interacts directly with several other
CC division proteins. {ECO:0000256|HAMAP-Rule:MF_00909}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}.
CC Note=Assembles at midcell at the inner surface of the cytoplasmic
CC membrane. {ECO:0000256|HAMAP-Rule:MF_00909}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000256|ARBA:ARBA00009690,
CC ECO:0000256|HAMAP-Rule:MF_00909, 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:OHT43316.1}.
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DR EMBL; MIKE01000028; OHT43316.1; -; Genomic_DNA.
DR RefSeq; WP_026110047.1; NZ_MUHH01000032.1.
DR AlphaFoldDB; A0A1S1J257; -.
DR STRING; 1278819.BHE19_18650; -.
DR OrthoDB; 9813375at2; -.
DR Proteomes; UP000180252; Unassembled WGS sequence.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-UniRule.
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; PS01134; FTSZ_1; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00909,
KW ECO:0000256|RuleBase:RU000631};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00909,
KW ECO:0000256|RuleBase:RU000631};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00909};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00909};
KW Septation {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}.
FT DOMAIN 21..213
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 216..334
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 641..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 117..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT BINDING 195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ SEQUENCE 675 AA; 74003 MW; 8D723FD40AD0DE87 CRC64;
MMSNSEFGSI SFDLPKNQSN VIKVIGVGGG GSNAINHMFK QGIKGVDFIV CNTDSQALQN
SSVPNKIQLG MNLTEGLGAG ANPDVGQQSA IESIADIEKM LDRGTKMVFI TAGMGGGTGT
GAAPVIAQLA KEREILTVGI VTIPFQFEGK VRQEQALLGI EKLRKQVDSL IVINNNKLRE
VYGNLGFKAG FSKADEVLAT ASRGIAEVIT HHYTQNIDLR DAKTVLSNSG TAIMGSSVAE
GENRAKEAII AALDSPLLND NKITGAKNVL LLIVSGSNEI TLDEIGEIND HIQAEAGYNA
NIIMGVGEDE TLGEAIAVTI IATGFDVEQQ NDIVNTEPKK IIHTLEDEQR SVHNLTNKSV
TSFDLTIDTP TSKSEEKIVF DLMDDEDTVA PVTPAPVVPV AATPFEVAPV AATPTMNQEE
LVVMSEFIKN LDVTFEIVSP ITDIDFTITT PQAEAFQDIK PVQQVQQRTF EREEQTTFSF
DLPIFRSEPE VRKEPVVEET KVLFELTNET RNIKVNDPVS FVPVTELSDK GVIKYSLEEY
MEVENDLMTS KPVEKVVEEV IPAELNITMK PRPDFAVEPD YSTTANVSPM ELTIEETLRL
RAEERRKKLK EFNYKFHNNV SRIDELEKEP AYKRLGIDLS NSQANNTNSR ISVGTDSNND
LQLRSNNSFL HDNVD
//
