FTSE_MYCTU
ID FTSE_MYCTU Reviewed; 230 AA.
AC O05779; F2GNW5; I6XG74; P96292; Q7D645;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cell division ATP-binding protein FtsE;
GN Name=ftsE {ECO:0000303|PubMed:8921846};
GN OrderedLocusNames=Rv3102c {ECO:0000312|EMBL:CCP45912.1},
GN RVBD_3102c {ECO:0000312|EMBL:AFN51094.1},
GN LH57_16935 {ECO:0000312|EMBL:AIR15884.1};
GN ORFNames=P425_03233 {ECO:0000312|EMBL:KBJ29148.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genome Sequencing Platform;
RA Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-230.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8921846; DOI=10.1016/0378-1119(96)00271-5;
RA Tyagi J.S., Das T.K., Kinger A.K.;
RT "An M. tuberculosis DNA fragment contains genes encoding cell division
RT proteins ftsX and ftsE, a basic protein and homologues of PemK and small
RT protein B.";
RL Gene 177:59-67(1996).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular
CC division. Has ATPase activity. {ECO:0000250|UniProtKB:A5U7B7,
CC ECO:0000250|UniProtKB:P0A9R7}.
CC -!- SUBUNIT: Homodimer. Forms a membrane-associated complex with FtsX.
CC {ECO:0000250|UniProtKB:A5U7B7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A5U7B7};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:A5U7B7}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:A5U7B7}. Note=Associated with the membrane
CC through an interaction with FtsX. {ECO:0000250|UniProtKB:A5U7B7}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFN51094.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
CC Sequence=AIR15884.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
CC Sequence=CCP45912.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
CC Sequence=KBJ29148.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
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DR EMBL; AL123456; CCP45912.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP003248; AFN51094.1; ALT_INIT; Genomic_DNA.
DR EMBL; JLDD01000038; KBJ29148.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP009480; AIR15884.1; ALT_INIT; Genomic_DNA.
DR EMBL; X70031; CAA49619.1; -; Genomic_DNA.
DR RefSeq; NP_217618.1; NC_000962.3.
DR AlphaFoldDB; O05779; -.
DR SMR; O05779; -.
DR STRING; 83332.Rv3102c; -.
DR PaxDb; O05779; -.
DR PRIDE; O05779; -.
DR DNASU; 888672; -.
DR GeneID; 888672; -.
DR KEGG; mtu:Rv3102c; -.
DR KEGG; mtv:RVBD_3102c; -.
DR PATRIC; fig|83332.111.peg.3456; -.
DR TubercuList; Rv3102c; -.
DR eggNOG; COG2884; Bacteria.
DR HOGENOM; CLU_000604_1_22_11; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..230
FT /note="Cell division ATP-binding protein FtsE"
FT /id="PRO_0000432514"
FT DOMAIN 3..228
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 36..37
FT /note="IG -> DR (in Ref. 5; CAA49619)"
FT /evidence="ECO:0000305"
FT CONFLICT 99..100
FT /note="YD -> SH (in Ref. 5; CAA49619)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> E (in Ref. 5; CAA49619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 25728 MW; 530680D0751A109F CRC64;
MMITLDHVTK QYKSSARPAL DDINVKIDKG EFVFLIGPSG SGKSTFMRLL LAAETPTSGD
VRVSKFHVNK LRGRHVPKLR QVIGCVFQDF RLLQQKTVYD NVAFALEVIG KRTDAINRVV
PEVLETVGLS GKANRLPDEL SGGEQQRVAI ARAFVNRPLV LLADEPTGNL DPETSRDIMD
LLERINRTGT TVLMATHDHH IVDSMRQRVV ELSLGRLVRD EQRGVYGMDR
