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Database: UniProt
Entry: E8UT08_THEBF
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ID   E8UT08_THEBF            Unreviewed;       708 AA.
AC   E8UT08;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Cell division protein FtsK/SpoIIIE {ECO:0000313|EMBL:ADV79798.1};
GN   OrderedLocusNames=Thebr_1224 {ECO:0000313|EMBL:ADV79798.1};
OS   Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 /
OS   AKO-1) (Thermoanaerobacter finnii).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV79798.1, ECO:0000313|Proteomes:UP000002062};
RN   [1] {ECO:0000313|EMBL:ADV79798.1, ECO:0000313|Proteomes:UP000002062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC   {ECO:0000313|Proteomes:UP000002062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC       {ECO:0000256|ARBA:ARBA00025923}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; CP002466; ADV79798.1; -; Genomic_DNA.
DR   RefSeq; WP_004396224.1; NC_014964.1.
DR   AlphaFoldDB; E8UT08; -.
DR   KEGG; tbo:Thebr_1224; -.
DR   HOGENOM; CLU_001981_9_6_9; -.
DR   Proteomes; UP000002062; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 3.30.980.40; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR025199; FtsK_4TM.
DR   InterPro; IPR041027; FtsK_alpha.
DR   InterPro; IPR002543; FtsK_dom.
DR   InterPro; IPR018541; Ftsk_gamma.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   Pfam; PF13491; FtsK_4TM; 1.
DR   Pfam; PF17854; FtsK_alpha; 1.
DR   Pfam; PF09397; FtsK_gamma; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00843; Ftsk_gamma; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50901; FTSK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:ADV79798.1};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        51..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        144..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          377..564
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         394..401
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   708 AA;  78576 MW;  FC14008F086FAE5C CRC64;
     MIDKKQKSLK NEIIGIIFLA FTLISFLSLY TDTTGAIGKN IGIFLKGSFG IGSYVVSALL
     LVFALMFLFN NRDFIKLHKA AALFGLFLTL ISLDHLYYFP SNEGLKNYIL AAYTNGINNM
     GGGVVAALLV YFLVKLLGIT GSYILLFSSL AIFIVLITNV SIVNLMESSY QKFKQRKKKI
     KKTDHEKEVI STSTSQEDFT PLIEENITDK NRTIDIIEQV EEERKIYEKG TKDKEEVIES
     EYLPPPITLL KEAIPPPKIK NEVLMEKVKK IEDTLKNFGV DAKVIQVTKG PAITRFELQP
     SAGVKVSRIV SLTDDIALSL AAPSVRIEAP IPGKSAIGIE VPNDKIAPVY LREVIDSKKF
     RNFKSGLAIG LGKDIAGNIV IADLSKMPHL LIAGATGSGK SVCINSLIVS LLYKAPPQQV
     KMILIDPKVV ELNIYNGIPH LLTPVVTDPK KAAGVLNWAV QEMTKRYNLF AQYGVRDIDS
     YNEKYKENSL YKIVIIIDEL SDLMMVSPAE VEEYIFRLAQ MARAAGIHLV IATQRPSVDV
     ITGVIKANIP SRISFAVSSQ IDSRTILDMT GAEKLLGKGD MLFNPIGAAK PMRIQGAFIS
     EEEVEAVVNF LKNHSKPQYE EIEIEEKTNG KIFEQQEDEL LEDAISVILE TGQASISMLQ
     RRLRIGYARA ARIIDQLEQK GIISGYDGSK PRQILLSKEE IKKILEES
//
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