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Database: UniProt
Entry: G2MWK9_9THEO
LinkDB: G2MWK9_9THEO
Original site: G2MWK9_9THEO 
ID   G2MWK9_9THEO            Unreviewed;       704 AA.
AC   G2MWK9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN   ORFNames=Thewi_1335 {ECO:0000313|EMBL:AEM78757.1};
OS   Thermoanaerobacter wiegelii Rt8.B1.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=697303 {ECO:0000313|EMBL:AEM78757.1, ECO:0000313|Proteomes:UP000008276};
RN   [1] {ECO:0000313|EMBL:AEM78757.1, ECO:0000313|Proteomes:UP000008276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rt8.B1 {ECO:0000313|EMBL:AEM78757.1,
RC   ECO:0000313|Proteomes:UP000008276};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Daligault H., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hemme C.,
RA   Woyke T.;
RT   "Complete sequence of Thermoanaerobacter wiegelii Rt8.B1.";
RL   Submitted (AUG-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; CP002991; AEM78757.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2MWK9; -.
DR   STRING; 697303.Thewi_1335; -.
DR   KEGG; twi:Thewi_1335; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_1030295_0_0_9; -.
DR   Proteomes; UP000008276; 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:0007049; P:cell cycle; 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};
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   704 AA;  78181 MW;  BA03DF9BF0D010F1 CRC64;
     MIDKKQKSLK NEIIGIIFLA FTLISFLSLY TDTTGAIGKN IGIFLKGSFG IGSYVVSALL
     LVFALMFLFN NRDFIKLHKA AALFGLFLTL ISLDHLYYFP SNEGLKNYIL AAYTNGINNM
     GGGVVAALLV YFLVKLLGIT GSYILLFSSL AIFIVLITNV SIVNLMESSY QKFKQRKKKI
     KKTDHEKEVI STSTSQEDFT PLIEENITEK 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 IKKY
//
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