FTSZ1_RHIME
ID FTSZ1_RHIME Reviewed; 590 AA.
AC P30327;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cell division protein FtsZ 1 {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ1 {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=R02168;
GN ORFNames=SMc01874;
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=1653222; DOI=10.1128/jb.173.18.5822-5830.1991;
RA Margolin W., Corbo J.C., Long S.R.;
RT "Cloning and characterization of a Rhizobium meliloti homolog of the
RT Escherichia coli cell division gene ftsZ.";
RL J. Bacteriol. 173:5822-5830(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=9352931; DOI=10.1128/jb.179.21.6788-6797.1997;
RA Ma X., Sun Q., Wang R., Singh G., Jonietz E.L., Margolin W.;
RT "Interactions between heterologous FtsA and FtsZ proteins at the FtsZ
RT ring.";
RL J. Bacteriol. 179:6788-6797(1997).
RN [3]
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 [4]
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; AF024660; AAC45824.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC46747.1; -; Genomic_DNA.
DR PIR; A38119; A38119.
DR RefSeq; NP_386274.1; NC_003047.1.
DR RefSeq; WP_010969741.1; NC_003047.1.
DR AlphaFoldDB; P30327; -.
DR SMR; P30327; -.
DR STRING; 266834.SMc01874; -.
DR EnsemblBacteria; CAC46747; CAC46747; SMc01874.
DR GeneID; 61603632; -.
DR KEGG; sme:SMc01874; -.
DR PATRIC; fig|266834.11.peg.3634; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_5_1_5; -.
DR OMA; FRPQSKI; -.
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; IPR017844; Cell_div_FtsZ_C.
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 TIGRFAMs; TIGR03483; FtsZ_alphas_C; 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..590
FT /note="Cell division protein FtsZ 1"
FT /id="PRO_0000114373"
FT REGION 346..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 111..113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
SQ SEQUENCE 590 AA; 62975 MW; 11B046DF0FA7B8F5 CRC64;
MAINLQKPDI TELKPRITVF GVGGGGGNAV NNMITAGLQG VDFVVANTDA QALTMTKAER
IIQMGVAVTE GLGAGSQPEV GRAAAEECID EIIDHLQGTH MCFVTAGMGG GTGTGAAPIV
AQAARNKGIL TVGVVTKPFH FEGGRRMRIA DQGISDLQKS VDTLIVIPNQ NLFRIANDKT
TFADAFAMAD QVLYSGVACI TDLMVKEGLI NLDFADVRSV MREMGRAMMG TGEASGEGRA
MAAAEAAIAN PLLDETSMKG AQGLLISITG GRDLTLFEVD EAATRIREEV DPDANIILGA
TFDEELEGLI RVSVVATGID RTAAEVAGRS ADFRPVAPKP IVRPSAAVPA QPQPTVSLQP
VPQPQPVQQP LQQQNVDHIA LAIREAEMER ELDIAARAQV AAPAPQPQPH LQEEAFRPQS
KLFAGVAPTE AAPVMRPAQP APRPVEMQAP VQPQMQAQPV QQEPTQVVRQ QAEPVRMPKV
EDFPPVVKAE MDYRTQPAPA HQEERGPMGL LNRITSSLGL REREATNVSS DMTAAAPSAA
SQQRRPLSPE ASLYAPRRGQ LDDHGRAAPQ MRSHEDDQLE IPAFLRRQSS
