ID K1Z0I3_9BACT Unreviewed; 319 AA.
AC K1Z0I3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=Cell division protein FtsZ {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=ACD_72C00551G0001 {ECO:0000313|EMBL:EKD42861.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD42861.1};
RN [1] {ECO:0000313|EMBL:EKD42861.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- SIMILARITY: Belongs to the FtsZ family.
CC {ECO:0000256|ARBA:ARBA00009690}.
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:EKD42861.1}.
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DR EMBL; AMFJ01029530; EKD42861.1; -; Genomic_DNA.
DR AlphaFoldDB; K1Z0I3; -.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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; 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; IPR017975; Tubulin_CS.
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; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 1..133
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 135..252
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 277..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 319
FT /evidence="ECO:0000313|EMBL:EKD42861.1"
SQ SEQUENCE 319 AA; 34007 MW; 59A127B3EFC95501 CRC64;
MDPEVGRKAA EESQNEIRDM LKDSDMVFIT CGLGGGTGSG ASAVVAEVAK ELGALTVAVV
TKPFGFEGPK RRDIADSAWN KLAHNVDAII TIPNDRILQV IDKKTSLLDA FRIVDDVLQQ
GVQGISEIIT TPSLINVDFA DVKTIMRDTG SALMGIGTGT GENRAIDAAK MAISSPLLEL
SIDGAHGILF TIAGGADLGM NEVSEAAKII TSSAAEDAKV IFGTTIDDTL AGSVRITVIA
TGFDERNSLL SSNEDEAPSF FSANKFTSTN FLRKAQKEEE EEEKKFKQFT QVAPKPVQAS
TPVMNDWAPK EDLQRSTPV
//