ID A0A1I0V7N6_9FIRM Unreviewed; 913 AA.
AC A0A1I0V7N6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:SFA72351.1};
GN ORFNames=SAMN05216249_101207 {ECO:0000313|EMBL:SFA72351.1};
OS Acetitomaculum ruminis DSM 5522.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetitomaculum.
OX NCBI_TaxID=1120918 {ECO:0000313|EMBL:SFA72351.1, ECO:0000313|Proteomes:UP000198838};
RN [1] {ECO:0000313|EMBL:SFA72351.1, ECO:0000313|Proteomes:UP000198838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5522 {ECO:0000313|EMBL:SFA72351.1,
RC ECO:0000313|Proteomes:UP000198838};
RA de Groot N.N.;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOJY01000001; SFA72351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0V7N6; -.
DR STRING; 1120918.SAMN05216249_101207; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000198838; 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 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:UP000198838};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 563..759
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 580..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 913 AA; 101675 MW; EFB0305FC65E613C CRC64;
MAARKASKSR SARKKRSTSG KKNNSVQNKQ FDKLILNTVV PAVSFGLCVF LEITLFGLGG
IAGKKIAEVC FGLFGFFAYL MPIALFTLIC FNIANKGNIV AKIKTIASVF FLWGLCVFAQ
LCSKGYVETQ DYMAYYDASV QSKAMGGLVG GSVVKLLFPL IGGFGLFILD FSVIFVSFII
ISEKSLFSDI YQLYKTKKKS RKKQEKKSSK KKPRREKEYV EEKPQKNINK ENKKKSVLYS
IPTMDFKEEE EKLAQELASD EADKQAVSSS TNQKEEETDL KNSVLDDFTD YSPKPIDADL
SVEDGLLDEE LTVEISKDDF LEKLSKDKKE DFEEDLPINE ESLDDEILID DIIIDTDEIS
KEALEDGNTL SDDRVFEINV EEDDDDIIPL DTEILNPDDI KPIETETLMH NETEESTEKA
SVSASKYEFP PIDFLEKGNS DSAMDSRTKI AETGKRLVET LRNFGVKVTL IGASCGPTVT
RYELKPEQGV KVSKILGLTD DIKLNLAATD VRIEAPIPGK AAIGIEVPNE HVVSVPLREL
LESKEFEEFK PKLAFAVGKD IAGKNVICDI SKMPHLLIAG ATGSGKSVCI NTIIMSILYK
ARPDEVKMIL IDPKVVELSI YKGIPHLINN EVVSKPDRAI GVLKWAEKEM DDRYEHFVQY
GVRNIKGYNE KAEKSQNTDQ PMKKMYQLLI VIDELADLMM LASKEVENSI QRLTQLARAA
GIHLVLATQR PSVNVITGVI KANMASRLAF AVSSGIDSRT ILDCVGAERL LGKGDMLFYP
QDYAKPQRLQ GPFVSDDEII KVVDFLKSKS VPEEEEVKAN FEEYIVTNPS GSKSKSDNDV
DPLFVEAGQL IIRKKKASIG MLQRTLSVGF NRAARIMDQL CFAGVVGGEE GTKPRKILMD
EVGFLQYVQE NNL
//
