FTSE_MYCTA
ID FTSE_MYCTA Reviewed; 229 AA.
AC A5U7B7;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cell division ATP-binding protein FtsE {ECO:0000305};
GN Name=ftsE {ECO:0000303|PubMed:16416128};
GN OrderedLocusNames=MRA_3134 {ECO:0000312|EMBL:ABQ74917.1};
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
RN [2]
RP SUBUNIT, INTERACTION WITH FTSX, SUBCELLULAR LOCATION, ATP-BINDING, AND
RP MUTAGENESIS OF LYS-42.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=16416128; DOI=10.1007/s00203-005-0079-z;
RA Mir M.A., Rajeswari H.S., Veeraraghavan U., Ajitkumar P.;
RT "Molecular characterisation of ABC transporter type FtsE and FtsX proteins
RT of Mycobacterium tuberculosis.";
RL Arch. Microbiol. 185:147-158(2006).
RN [3]
RP FUNCTION AS AN ATPASE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MUTAGENESIS OF LYS-42 AND CYS-84.
RX PubMed=25511207; DOI=10.1007/s10930-014-9593-7;
RA Mir M.A., Arumugam M., Mondal S., Rajeswari H.S., Ramakumar S.,
RA Ajitkumar P.;
RT "Mycobacterium tuberculosis cell division protein, FtsE, is an ATPase in
RT dimeric form.";
RL Protein J. 34:35-47(2015).
CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular
CC division (By similarity). Has ATPase activity (PubMed:25511207).
CC {ECO:0000250|UniProtKB:P0A9R7, ECO:0000269|PubMed:25511207}.
CC -!- ACTIVITY REGULATION: Requires magnesium or manganese for optimal
CC activity. Inhibited by high concentrations of cobalt and by cupric
CC phenanthroline. {ECO:0000269|PubMed:25511207}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 uM for ATP {ECO:0000269|PubMed:25511207};
CC Vmax=0.57 nmol/min/mg enzyme {ECO:0000269|PubMed:25511207};
CC pH dependence:
CC Optimum pH is 7.4-7.8 for ATPase activity.
CC {ECO:0000269|PubMed:25511207};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius for ATPase activity.
CC {ECO:0000269|PubMed:25511207};
CC -!- SUBUNIT: Homodimer (PubMed:16416128, PubMed:25511207). Forms a
CC membrane-associated complex with FtsX (PubMed:16416128).
CC {ECO:0000269|PubMed:16416128, ECO:0000269|PubMed:25511207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16416128};
CC Peripheral membrane protein {ECO:0000269|PubMed:16416128}; Cytoplasmic
CC side {ECO:0000269|PubMed:16416128}. Note=Associated with the membrane
CC through an interaction with FtsX. {ECO:0000269|PubMed:16416128}.
CC -!- MISCELLANEOUS: The active form is a dimer, wherein the participating
CC monomers are held together by non-covalent interactions, with the Cys-
CC 84 of each monomer present at the dimer interface. In vitro, under
CC oxidizing environment, the dimer gets stabilized by the formation of
CC Cys-84-Cys-84 disulfide bond. {ECO:0000305|PubMed:25511207}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; CP000611; ABQ74917.1; -; Genomic_DNA.
DR RefSeq; WP_003416120.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U7B7; -.
DR SMR; A5U7B7; -.
DR STRING; 419947.MRA_3134; -.
DR EnsemblBacteria; ABQ74917; ABQ74917; MRA_3134.
DR GeneID; 45427101; -.
DR KEGG; mra:MRA_3134; -.
DR eggNOG; COG2884; Bacteria.
DR HOGENOM; CLU_000604_1_22_11; -.
DR OMA; LPMYQRA; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000001988; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR005286; Cell_div_FtsE_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02673; FtsE; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding.
FT CHAIN 1..229
FT /note="Cell division ATP-binding protein FtsE"
FT /id="PRO_0000432742"
FT DOMAIN 2..227
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16416128"
FT MUTAGEN 42
FT /note="K->R: Does not bind ATP. Does not affect
FT dimerization."
FT /evidence="ECO:0000269|PubMed:16416128,
FT ECO:0000269|PubMed:25511207"
FT MUTAGEN 84
FT /note="C->A: Does not affect ATPase activity."
FT /evidence="ECO:0000269|PubMed:25511207"
SQ SEQUENCE 229 AA; 25596 MW; 2F6BF50728761AA0 CRC64;
MITLDHVTKQ YKSSARPALD DINVKIDKGE FVFLIGPSGS GKSTFMRLLL AAETPTSGDV
RVSKFHVNKL RGRHVPKLRQ VIGCVFQDFR LLQQKTVYDN VAFALEVIGK RTDAINRVVP
EVLETVGLSG KANRLPDELS GGEQQRVAIA RAFVNRPLVL LADEPTGNLD PETSRDIMDL
LERINRTGTT VLMATHDHHI VDSMRQRVVE LSLGRLVRDE QRGVYGMDR
