FTSZ_CORGL
ID FTSZ_CORGL Reviewed; 442 AA.
AC P94337; O24746;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN OrderedLocusNames=Cgl2155, cg2366;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9240446; DOI=10.1006/bbrc.1997.6930;
RA Kobayashi M., Asai Y., Hatakeyama K., Kijima N., Wachi M., Nagai K.,
RA Yukawa H.;
RT "Cloning, sequencing, and characterization of the ftsZ gene from coryneform
RT bacteria.";
RL Biochem. Biophys. Res. Commun. 236:383-388(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=9738885; DOI=10.1007/s004380050793;
RA Honrubia M.P., Fernandez F.J., Gil J.A.;
RT "Identification, characterization, and chromosomal organization of the ftsZ
RT gene from Brevibacterium lactofermentum.";
RL Mol. Gen. Genet. 259:97-104(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; AB003132; BAA21687.1; -; Genomic_DNA.
DR EMBL; Y08964; CAA70158.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99548.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20495.1; -; Genomic_DNA.
DR PIR; JC5548; JC5548.
DR RefSeq; NP_601357.1; NC_003450.3.
DR RefSeq; WP_011014920.1; NC_006958.1.
DR PDB; 6SAT; X-ray; 1.60 A; P/Q=433-442.
DR PDB; 6SCS; X-ray; 2.20 A; P/Q/R/S=433-442.
DR PDBsum; 6SAT; -.
DR PDBsum; 6SCS; -.
DR AlphaFoldDB; P94337; -.
DR SMR; P94337; -.
DR STRING; 196627.cg2366; -.
DR World-2DPAGE; 0001:P94337; -.
DR PRIDE; P94337; -.
DR KEGG; cgb:cg2366; -.
DR KEGG; cgl:Cgl2155; -.
DR PATRIC; fig|196627.13.peg.2093; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_2_3_11; -.
DR OMA; GNPSIGQ; -.
DR Proteomes; UP000000582; 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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; GTP-binding;
KW Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..442
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114348"
FT REGION 329..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 105..107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT BINDING 184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT CONFLICT 21
FT /note="V -> D (in Ref. 1; BAA21687)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="D -> Y (in Ref. 1; BAA21687)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="T -> A (in Ref. 1; BAA21687)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..116
FT /note="AG -> GR (in Ref. 1; BAA21687)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="A -> R (in Ref. 2; CAA70158)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..203
FT /note="GV -> C (in Ref. 1; BAA21687)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="S -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="Q -> QQ (in Ref. 1; BAA21687)"
FT /evidence="ECO:0000305"
FT CONFLICT 410..413
FT /note="Missing (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:6SAT"
SQ SEQUENCE 442 AA; 47214 MW; 9D764FEC262E6073 CRC64;
MTSPNNYLAK IKVVGVGGGG VNAVNRMIEE GLKGVEFIAV NTDSQALMFS DADVKLDIGR
EATRGLGAGA NPEVGRASAE DHKNEIEETI KGADMVFVTA GEGGGTGTGA APVVAGIAKK
MGALTIGVVT KPFEFEGRRR TRQAEEGIAA LKEVCDTLIV IPNDRLLELG DANLSIMEAF
RAADEVLHNG VQGITNLITI PGVINVDFAD VRSVMSEAGS ALMGVGSARG DNRVVSATEQ
AINSPLLEAT MDGATGVLLS FAGGSDLGLM EVNAAASMVR ERSDEDVNLI FGTIIDDNLG
DEVRVTVIAT GFDAARASAA ENRRAGISAA PAAEPVQQQV PTTNATLPPE KESIFGGARE
ENDPYLSRSA GARHRIEETR SGGGLFTTGN DRDYRRDERR EDHRDERRDE RRDDRSYDRR
DDRRDDRRDD RGDDLDVPSF LQ
