FTSZB_DICDI
ID FTSZB_DICDI Reviewed; 366 AA.
AC Q9GPZ7; Q55C22;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mitochondrial division protein fszB;
GN Name=fszB; Synonyms=ftsZB; ORFNames=DDB_G0269224;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=14665465; DOI=10.1128/ec.2.6.1315-1326.2003;
RA Gilson P.R., Yu X.-C., Hereld D., Barth C., Savage A., Kiefel B.R., Lay S.,
RA Fisher P.R., Margolin W., Beech P.L.;
RT "Two Dictyostelium orthologs of the prokaryotic cell division protein FtsZ
RT localize to mitochondria and are required for the maintenance of normal
RT mitochondrial morphology.";
RL Eukaryot. Cell 2:1315-1326(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probably involved in mitochondrion division process. Binds to
CC and hydrolyzes GTP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14665465}.
CC Note=Locates to a submitochondrial body usually located at one end of
CC the organelle.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000305}.
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DR EMBL; AF304441; AAG37881.1; -; Genomic_DNA.
DR EMBL; AAFI02000005; EAL71962.1; -; Genomic_DNA.
DR RefSeq; XP_646659.1; XM_641567.1.
DR AlphaFoldDB; Q9GPZ7; -.
DR SMR; Q9GPZ7; -.
DR STRING; 44689.DDB0191117; -.
DR PaxDb; Q9GPZ7; -.
DR EnsemblProtists; EAL71962; EAL71962; DDB_G0269224.
DR GeneID; 8617631; -.
DR KEGG; ddi:DDB_G0269224; -.
DR dictyBase; DDB_G0269224; fszB.
DR eggNOG; ENOG502QRFN; Eukaryota.
DR HOGENOM; CLU_024865_0_1_1; -.
DR InParanoid; Q9GPZ7; -.
DR OMA; GNPSIGQ; -.
DR PhylomeDB; Q9GPZ7; -.
DR PRO; PR:Q9GPZ7; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:dictyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:dictyBase.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; IMP:dictyBase.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IMP:dictyBase.
DR GO; GO:0048285; P:organelle fission; IBA:GO_Central.
DR CDD; cd02201; FtsZ_type1; 1.
DR Gene3D; 3.40.50.1440; -; 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; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 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; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR TIGRFAMs; TIGR00065; ftsZ; 1.
DR PROSITE; PS01134; FTSZ_1; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Reference proteome.
FT CHAIN 1..366
FT /note="Mitochondrial division protein fszB"
FT /id="PRO_0000327693"
FT BINDING 70..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 157..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
SQ SEQUENCE 366 AA; 39943 MW; 3F3351F6C6366987 CRC64;
MTILNRFCRT ILLTNLELTN CGIRKNNSYK CRSFTHTINI DTNHIVPIHT QSNITLELFQ
PKISVVGVGG GGGNAVNHMI SQSLEGVEFF VCNTDSQDLI KSNSINKIQL GPQLTKGHGA
GANPEKGRLA AEESKNKIIQ TFKDTDLLFL AAGMGGGTGT GSSPIIAKTI KEFKKETIIV
GVVTVPFNFE GKRKEIIAKK GLEELSKYVD TLVVISNQNL LDASKSDIQL EQAFLMVDEI
LHTGIRSIAN IINVPGMINL DYSDVVNILK NRKGLSRIGF GEASGEDRAY KAVHKAIKNP
LIEIDDQKFT GLLVNISGGN DITLNEISKT INYLQQNADP DVQVFVGHTV DNSLLGKIRI
SCLFVH
