(data stored in SCRATCH zone)

SWISSPROT: A4ATL3_MARSH

ID   A4ATL3_MARSH            Unreviewed;       639 AA.
AC   A4ATL3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 83.
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   OrderedLocusNames=FB2170_16901 {ECO:0000313|EMBL:EAR00783.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00783.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00783.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Essential cell division protein that forms a contractile
CC       ring structure (Z ring) at the future cell division site. The
CC       regulation of the ring assembly controls the timing and the
CC       location of cell division. One of the functions of the FtsZ ring
CC       is to recruit other cell division proteins to the septum to
CC       produce a new cell wall between the dividing cells. Binds GTP and
CC       shows GTPase activity. {ECO:0000256|HAMAP-Rule:MF_00909,
CC       ECO:0000256|RuleBase:RU000631}.
CC   -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure
CC       in a strictly GTP-dependent manner. Interacts directly with
CC       several other division proteins. {ECO:0000256|HAMAP-
CC       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:RU000631}.
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DR   EMBL; CP002157; EAR00783.1; -; Genomic_DNA.
DR   RefSeq; WP_013304586.1; NC_014472.1.
DR   STRING; 313603.FB2170_16901; -.
DR   EnsemblBacteria; EAR00783; EAR00783; FB2170_16901.
DR   KEGG; fbc:FB2170_16901; -.
DR   eggNOG; ENOG4105CDK; Bacteria.
DR   eggNOG; COG0206; LUCA.
DR   HOGENOM; HOG000049094; -.
DR   KO; K03531; -.
DR   OMA; HGANIIM; -.
DR   OrthoDB; 1009041at2; -.
DR   BioCyc; MSP313603:G1GNS-158-MONOMER; -.
DR   Proteomes; UP000001602; 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.
DR   PROSITE; PS01135; FTSZ_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATL3.
DR   SWISS-2DPAGE; A4ATL3.
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, ECO:0000313|EMBL:EAR00783.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Septation {ECO:0000256|HAMAP-Rule:MF_00909,
KW   ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN       21    213       Tubulin. {ECO:0000259|SMART:SM00864}.
FT   DOMAIN      216    334       Tubulin_C. {ECO:0000259|SMART:SM00865}.
FT   NP_BIND      29     33       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   NP_BIND     117    119       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     148    148       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     152    152       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
FT   BINDING     195    195       GTP. {ECO:0000256|HAMAP-Rule:MF_00909}.
SQ   SEQUENCE   639 AA;  70161 MW;  C4204865B44D0197 CRC64;
     MSKNTEIESI SFDLPKNQSN VIKVIGVGGG GSNAINHMFE AGINGVDFVI CNTDSQALEN
     SAVPNKIQLG VSLTEGLGAG ANPEVGEQAA IESMEDIKTM LDNTTKMIFI TAGMGGGTGT
     GAAPVIAKQA KEMDVLTVGI VTMPFQFEGK MRCQQAQLGI EKLRANVDSL IVINNNKLRE
     VYGNLGFKAG FSKADEVLAT AARGIAEVIT HHYTQNIDLR DAKTVLSNSG TAIMGSAMAS
     GSSRANEAIM KALDSPLLND NKISGAKNVL LLIVSGSQEI TIDEIGEIND HIQAEAGHGA
     NIIMGVGEDD TLGEAIAVTV IATGFNLDQQ DDIVNTESKK IIHTLEEEQK AEQDLTPKNI
     VHQLVEEEEN DEPQMITEIE ELDGLDLIPT TNYIKNFNVF YEEVVAENVS EDDFVIFDAK
     DSVKDIEVVD PEVVSSKKIE EDQFAISFDL PLAESTEEDK ENVILFNLDD DVKDMDVNEH
     VEVIPVLEYN KEGETRYSLD DYMELENQLT GAKSKAEEFE PKIIEDELVF EKRTLGAEGE
     EAVTTAKTKE VDPMDSPIEE LLKERADERR RKLKDFNYKF QNGLSNIDEI EKEPAYKRQG
     VNLDENSIQN KVSRTTLSED SNDEIQLRSN NSFLHDNVD
//

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