(data stored in SCRATCH3701 zone)

SWISSPROT: D5E962_METMS

ID   D5E962_METMS            Unreviewed;       367 AA.
AC   D5E962;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU003360};
GN   Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909};
GN   OrderedLocusNames=Mmah_0178 {ECO:0000313|EMBL:ADE35713.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35713.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35713.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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}.
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|HAMAP-
CC       Rule:MF_00909, ECO:0000256|RuleBase:RU003360}.
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DR   EMBL; CP001994; ADE35713.1; -; Genomic_DNA.
DR   RefSeq; WP_013036656.1; NC_014002.1.
DR   EnsemblBacteria; ADE35713; ADE35713; Mmah_0178.
DR   GeneID; 8982309; -.
DR   KEGG; mmh:Mmah_0178; -.
DR   eggNOG; arCOG02201; Archaea.
DR   eggNOG; COG0206; LUCA.
DR   HOGENOM; HOG000049094; -.
DR   KO; K03531; -.
DR   OMA; GRRRANQ; -.
DR   OrthoDB; 41117at2157; -.
DR   BioCyc; MMAH547558:G1GHT-178-MONOMER; -.
DR   Proteomes; UP000001059; Chromosome.
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; -; 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; IPR024757; FtsZ_C.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR037103; Tubulin/FtsZ_C_sf.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
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.
PE   3: Inferred from homology;
DR   PRODOM; D5E962.
DR   SWISS-2DPAGE; D5E962.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU003360};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU003360, ECO:0000313|EMBL:ADE35713.1};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU003360};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU003360};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU003360}.
FT   DOMAIN          42..233
FT                   /note="Tubulin"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          235..352
FT                   /note="Tubulin_C"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NP_BIND         50..54
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   NP_BIND         137..139
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         168
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         172
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
FT   BINDING         215
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00909"
SQ   SEQUENCE   367 AA;  38212 MW;  8977460736F0ECF0 CRC64;
     MKSIVEEALA RSAEERQVSS EPSGPKDVNA EIEAVLKGMH TNIKVIGCGG GGSNSIQRMT
     NEGIKGAQLV ALNTDAQHLL NVICDNKILI GKKKTRGLGA GSLPQIGEDA ALESIDELTE
     VVDGTDMVFI TAGLGGGTGT GSAAVVAEAA RDAGALTIAV VTLPFAVEGE VRRTNAEAGL
     ERLRDVADTV IVVPNDKLLE VVPRLPLQAA FKVSDEVLMR AVKGITELIT KPGLVNLDFA
     DVRTVMQNGG VAMIGLGEAD GDSKASESVQ KALRSPLLDV DISGATSALV NVVGGQDMTV
     SEAEGVVQEV YSRIDPGARL IWGAQVDPEL EHTVRTMIVV TGVKSPQIYG PGGAKNVTRR
     YGIDFVG
//

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