ID A0A1M4M6Y0_9FIRM Unreviewed; 764 AA.
AC A0A1M4M6Y0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=DNA translocase ftsK {ECO:0000313|EMBL:SCG83392.1};
GN Name=ftsK {ECO:0000313|EMBL:SCG83392.1};
GN ORFNames=DW1_1824 {ECO:0000313|EMBL:SCG83392.1};
OS Proteiniborus sp. DW1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG83392.1, ECO:0000313|Proteomes:UP000185208};
RN [1] {ECO:0000313|EMBL:SCG83392.1, ECO:0000313|Proteomes:UP000185208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW1 {ECO:0000313|EMBL:SCG83392.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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; FMDO01000036; SCG83392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M4M6Y0; -.
DR STRING; 1889883.DW1_1824; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000185208; 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 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000185208};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 432..623
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 449..456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 764 AA; 84456 MW; 3D59140A9EE52761 CRC64;
MTKAKSRVTA KNKTTAKRDI KMEIMGILIV AVGLLSLLSM YNKSTGFIGQ IIKKYSIIIA
GLGGYVFPFI ILLVGFLFIT NKIELIKKTT SVIITYIGLL TILDINFFPF VEGLSFFDRV
KLSIEVNNSI IASESIASGG GIIGSALSYV FLRLFGTIGS YVVIAAIILI SFLLFTNISV
IDVTKNIFRR IVALIKATIN NTKDFVYVED KKGNTPSNKE DDIILKDMLS HDDKNNTSDS
SITTNEAETK IRVLDYTKSI DKSEQYAEKK HEDKLINRDN NIDIPEGQKN ESYDDYKLPS
TEILREVKSN SKNVEKKEVL NNANKLIETL HNFGIEAKIL QVSIGPSITR YEIQPAPGVK
VSKIVSLTND IALSLASSDI RMEAPIPGKS AIGIEVPNKN KVGVGLKEIL ESNEYKEIDT
LIPFALGKDI SGKPIVTNIE KMPHLLIAGA TGSGKSVCIN TLIASILYKA RPDQVKLMLI
DPKVVELSVY NGIPHLLIPV VTDPKKAAFS LNWAVQEMTR RYNLFAKNSV RDLDSYNNKA
ANNLEMEKLP KLVIIIDELA DLMMVSASEV EDYICRLAQM ARAAGIHLIV ATQRPSVDII
TGTIKANIPS RISFAVSSQA DSRTILDMGG AEKLLGKGDM LFYPVGESKP LRIQGAFIGE
EEINKLVEYL QSQCSANYEE KVVEEISNNL KQTTDDSDEL LPNAIDIVID EGQASISLLQ
RRLKIGYARA ARIIDEMEER GIVGGYEGSK PRKVLITRDE YEND
//