ID A0A1H7X9D3_9FIRM Unreviewed; 759 AA.
AC A0A1H7X9D3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:SEM29738.1};
GN ORFNames=SAMN04488698_101125 {ECO:0000313|EMBL:SEM29738.1};
OS Candidatus Frackibacter sp. WG12.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Frackibacter.
OX NCBI_TaxID=2017977 {ECO:0000313|EMBL:SEM29738.1, ECO:0000313|Proteomes:UP000199298};
RN [1] {ECO:0000313|Proteomes:UP000199298}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WG12 {ECO:0000313|Proteomes:UP000199298};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; FOCA01000001; SEM29738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7X9D3; -.
DR Proteomes; UP000199298; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 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; 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; 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 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..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 422..613
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 224..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439..446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 759 AA; 83945 MW; 23A3FEE0FE84A29C CRC64;
MISNTGDEVI KLKSALIKIY EERNDELLGI FLIVIAILLG VSLYFQATGV VGEILTRGFK
VIIGRGAYIL PFLFLLYGIN LIKSERIEVT VRVIGLIIMF VVVITILHLD VKPGTEFKFA
LEGKGGGIVG ALLLYILRQG LEEVGTYIVL GALGLIGFLL AANLFLANII SQIRDYIKSM
VDKLKVKFNK IQARWTQLRE QRKKEKRKVK KEIEEELDLQ EELKKNKQQS KNKLKKSISV
SNPNSENNKM KSSEVKDKEE DAKKQETKNE EQIREGNFNE VSEQTDDGYN LPPLSLLQPI
ENVDSSEVNQ ANSQVLEETL SSFGVEAEVV DVNYGPTITR YEIHPAPGVK VSKISNLSND
IALSLAASDV RIEAPIPGKA AVGIEVPNQE QVMVHLREIL ESSEFTESSS KLSVGLGKDI
AGKSIVADLS AMPHLLVAGA TGSGKSVCIN SIISSLLYKG SPEEIKMMLI DPKMVELAIY
NKIPHLIAPV VTDARKAAAA LKWVVEEMEN RYELFASNGA KGIKSYNQQF SAEEETKKLP
YIVVVIDELS DLMMVAANEV EDAICRLAQM ARAAGIHLII ATQRPSVDVI TGVIKANIPS
RISFAVSSQT DSRTILDTGG AEKLLGKGDM LFSPVGSQKA TRIQGAFISE SEVKDLVKYV
KEQENPEYAE KLEKIKDKEI TIETEDKDEL YEEAVKLVVD KRASISMLQR RLRIGYTRAA
RLIDTMEEEG IVGEHRGSKP REVLIDEDDL KELFNGEGG
//
