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FTSZ2_RHIME
ID   FTSZ2_RHIME             Reviewed;         346 AA.
AC   P45484;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Cell division protein FtsZ 2 {ECO:0000255|HAMAP-Rule:MF_00909};
GN   Name=ftsZ2 {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=R02051;
GN   ORFNames=SMc04296;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=8144471; DOI=10.1128/jb.176.7.2033-2043.1994;
RA   Margolin W., Long S.R.;
RT   "Rhizobium meliloti contains a novel second homolog of the cell division
RT   gene ftsZ.";
RL   J. Bacteriol. 176:2033-2043(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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:0000255|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:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}.
CC       Note=Assembles at midcell at the inner surface of the cytoplasmic
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00909}.
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DR   EMBL; L25440; AAA26281.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC46630.1; -; Genomic_DNA.
DR   PIR; S58854; S58854.
DR   RefSeq; NP_386157.1; NC_003047.1.
DR   RefSeq; WP_010969666.1; NC_003047.1.
DR   AlphaFoldDB; P45484; -.
DR   SMR; P45484; -.
DR   STRING; 266834.SMc04296; -.
DR   EnsemblBacteria; CAC46630; CAC46630; SMc04296.
DR   GeneID; 61603517; -.
DR   KEGG; sme:SMc04296; -.
DR   PATRIC; fig|266834.11.peg.3505; -.
DR   eggNOG; COG0206; Bacteria.
DR   HOGENOM; CLU_024865_0_2_5; -.
DR   OMA; GNPSIGQ; -.
DR   Proteomes; UP000001976; 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; 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   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   Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Reference proteome; Septation.
FT   CHAIN           1..346
FT                   /note="Cell division protein FtsZ 2"
FT                   /id="PRO_0000114374"
FT   REGION          320..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         23..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         110..112
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   CONFLICT        314
FT                   /note="Missing (in Ref. 1; AAA26281)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  36120 MW;  D8301BAF5D527EC7 CRC64;
     MTEYKKPIIT EMRPKITVIG VGGGGGNAIN NMIAENLQGV DFIAANTDAQ ALATSKAERR
     IQLGAAITEG LGAGSVPDIG NAAAQESIDE IMDHLGGTHM CFVTAGMGGG TGTGAAPVIA
     EAARRAGILT VAVVTKPFSF EGQRRMQTAE LGVERLRESA DTVIVIPNQN LFRIADAKTT
     FADAFMIADR VLYSGVSCIT DLIVKEGLMN LDFADVKTVM KGMGRAMMGT GEATGENRAM
     LAAEAAIANP LLDEVSMRGA KGVLVSISGG MDMTLFEVDE AATRIREEVY DEADIVVGAI
     FDRSLDGTFR VSVVATGLDS NRSAQPTAPE AMNGQTAAAV PSRTLQ
 
 
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