ID A0A0E4C8X6_9FIRM Unreviewed; 758 AA.
AC A0A0E4C8X6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=DNA translocase FtsK gamma {ECO:0000313|EMBL:CFX75910.1};
GN ORFNames=1811 {ECO:0000313|EMBL:CFX75910.1};
OS Syntrophomonas zehnderi OL-4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX75910.1, ECO:0000313|Proteomes:UP000045545};
RN [1] {ECO:0000313|EMBL:CFX75910.1, ECO:0000313|Proteomes:UP000045545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL-4 {ECO:0000313|EMBL:CFX75910.1,
RC ECO:0000313|Proteomes:UP000045545};
RA Murphy D.;
RL Submitted (MAR-2015) 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; CGIH01000029; CFX75910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E4C8X6; -.
DR STRING; 690567.1811; -.
DR Proteomes; UP000045545; 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:UP000045545};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 424..610
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 441..448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 758 AA; 83489 MW; C4284AC195B978D2 CRC64;
MEGNLHSMTN PKKKISSSQK KKPTAVRNAP PPKEKWALRE EVLSVVFFML AVFLFVSIRN
FQGIPEDRQF IGLIGTQLMI ALQLVFGRAA LLVSIFLLFW SIHLGVLKKI WSIRMWGLSL
LMLAIMIGMS LYNIPLGIDS WEAGLKGMGG GVIGGGAAYV LVRLVGQLGT SILLVLFTII
SLIMMLNKPI AEISRLVFNL AKRLKKMLNE LMFYEEPGIT EPPTAATKSE PLIIHPPVNT
VAEPEEIPYV APKPQVVTPL KPKLDEPQEG PKKEGPEIVF LGKEEPFEYR KPTLDMLGDL
GSERIIDKKN IKESISILED TFASFGVSVK VNQVSCGPAV TRYELTPAPG VKISRIISLT
DDLQLNLAAP GIRMEAPIPG KSAIGIEVPN AKITSVGLRS LIGSAQFSKL NSPLAVALGE
DIAGNAIVAR LSDMPHLLIA GSTGSGKSVC LNSIIMSFLY NATPDELKLV FIDPKMVELT
VYNGIPHLLT PVVTDPKKAS VILRWMTTEM EKRYKTFANK GVRDIYRYNQ TVEENMPFIV
IIIDELADLM MVSPMEVEDS ICRLAQMARA AGIHLIVATQ RPSVDVVTGI IKANIPSRIA
FAVSSQADSR TILDMGGAEK LLGKGDMLFF PVGAVKPYRV QGAFVSDSDI DKTVGFIKSQ
LPLNEAERLQ ELELNLDDMP IDADDEMFWE AVKIFVDSQK ASVSLLQRKL RVGYARAARL
VDAMEERGLV SEIDSNKKRE ILIDAEQLEK IYPQSKIF
//
