FTSZ_STAEQ
ID FTSZ_STAEQ Reviewed; 394 AA.
AC Q5HQ06;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=SERP0751;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 2-394 IN COMPLEX WITH GDP.
RC STRAIN=ATCC 35984 / RP62A;
RA Halavaty A.S., Minasov G., Winsor J., Dubrovska I., Filippova E.V.,
RA Olsen D.B., Therien A., Shuvalova L., Young K., Anderson W.F.;
RT "1.43 Angstrom resolution crystal structure of cell division protein FtsZ
RT (ftsZ) from Staphylococcus epidermidis RP62A in complex with GDP.";
RL Submitted (AUG-2013) to the PDB data bank.
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; CP000029; AAW54139.1; -; Genomic_DNA.
DR RefSeq; WP_002446230.1; NC_002976.3.
DR PDB; 4M8I; X-ray; 1.43 A; A=2-394.
DR PDBsum; 4M8I; -.
DR AlphaFoldDB; Q5HQ06; -.
DR SMR; Q5HQ06; -.
DR STRING; 176279.SERP0751; -.
DR EnsemblBacteria; AAW54139; AAW54139; SERP0751.
DR KEGG; ser:SERP0751; -.
DR eggNOG; COG0206; Bacteria.
DR HOGENOM; CLU_024865_0_1_9; -.
DR OMA; GNPSIGQ; -.
DR OrthoDB; 1009041at2; -.
DR Proteomes; UP000000531; 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..394
FT /note="Cell division protein FtsZ"
FT /id="PRO_0000114387"
FT REGION 317..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|Ref.2"
FT BINDING 29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 108..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|Ref.2"
FT BINDING 139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|Ref.2"
FT BINDING 143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT ECO:0000269|Ref.2"
FT BINDING 166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 97..108
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 179..202
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:4M8I"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:4M8I"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:4M8I"
SQ SEQUENCE 394 AA; 41411 MW; 9E7B5DD95849C544 CRC64;
MLEFEQGFNH LATLKVIGVG GGGNNAVNRM IDHGMNNVEF IAINTDGQAL NLSKAESKIQ
IGEKLTRGLG AGANPEIGKK AAEESREQIE DAIQGADMVF VTAGMGGGTG TGAAPVVAKI
AKEMGALTVG VVTRPFGFEG RKRQTQAAAG VESMKAAVDT LIVIPNDRLL DIVDKSTPMM
EAFKEADNVL RQGVQGISDL IAVSGEVNLD FADVKTIMSN QGSALMGIGV SSGENRAVEA
AKKAISSPLL ETSIVGAQGV LMNITGGESL SLFEAQEAAD IVQDAADEDV NMIFGTVINP
ELQDEIVVTV IATGFEDKPS SQGRKATSTG FGSSVNSSSN HQSGASAKED SFSAHTSHSQ
SSESVSERSH TTKDDDIPSF IRNREERRSR RTRR
