ID D4CK73_9FIRM Unreviewed; 1024 AA.
AC D4CK73;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:EFE92849.1};
GN ORFNames=GCWU000341_00743 {ECO:0000313|EMBL:EFE92849.1};
OS Oribacterium sp. oral taxon 078 str. F0262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=608534 {ECO:0000313|EMBL:EFE92849.1, ECO:0000313|Proteomes:UP000004602};
RN [1] {ECO:0000313|EMBL:EFE92849.1, ECO:0000313|Proteomes:UP000004602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0262 {ECO:0000313|EMBL:EFE92849.1,
RC ECO:0000313|Proteomes:UP000004602};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE92849.1}.
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DR EMBL; ACIQ02000009; EFE92849.1; -; Genomic_DNA.
DR AlphaFoldDB; D4CK73; -.
DR STRING; 608534.GCWU000341_00743; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_2_9; -.
DR Proteomes; UP000004602; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 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; 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 672..866
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 689..696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1024 AA; 110789 MW; B044BCAC86C70D0A CRC64;
MTAKGKSRKK REAESELKRQ AGGAGRSAGK NSVKAGGRGR TSSEKRKRGR KTAEKSAASR
SLSAAPSSDP EKASFREELL LLLALSLSIF LFLSNLGLCG PVGDLLRDLQ FGVFGLLGGL
LPFVLFFTTA LLLFAGEDQN SSRRLCAALL FLLFLGAFLQ LTAGGGVAGK DIREIYEEGA
SGGVGGGAVG GGIALLLWQA AGQAGALFLL FMGMLFCLVY ASGRPLLALL MGFSAGKVRE
AEEGIRRLSF ASEAGRRTTP APAAEREFTE IDLLQGEKTK PENLPPEEKR SGEESEEKGI
LDSFRDFIRG GESGEKEDAA ENSAASSLRI KGLHQEESSR PTEEKRDQGG EKEKAEEGRK
EIELPVLPGR RKRAQPAEDY LDSEPDYAKY GMWIEPEDDA WGHRGGADGD TGPSLPLTEA
AGPSGVRRRR ARMDSKRKRG IRGSRSFPSV SDEADIAKEG AGTESVSEEE LWIDEKEALS
RELHAAAPDP VRPSEERDRE KTGESRKAAD PSPREASESF GKEERGKPPR KGKEHSYHVP
PLSFLKTGGA QGADSREEIE RNALTLQKTL ESFGVGVSVS DVSVGPAVTR YELQPEQGVK
VSRIVSLSND IKMRLAASDI RIEAPIPGKS AVGIEVPNRN SQTVYLGDIL SSAEFRNAKM
ELSFGVGKDI EGKTVVTDIA KMPHLLIAGA TGSGKSVSIN TLIMSLIYRY SPEEVRMIMV
DPKVVELQVY NGIPHLLIPV VTDPKKAAAA LNWAVAEMSD RYKKFAEAGV RDLKGYNRRI
AELGGDAAAE KLPKIVIIID ELADLMMVSA QEVEEAICRI AQLARACGMH LVIATQRPSV
NVITGLIKAN VPSRIAFAVS SGVDSRTIID MNGAEKLLGK GDMLFFPQGI PKPVRVQGAF
VSDQEVQDAV EYLKEHTESD YSEELSSSIE NPLSGESRAE SDRDELFREA GELVTEAEKA
SIGMLQRRFR IGFNRAARIM DQLSDYGVVG AEEGTKGRKV QMTKEEFLSF LSEREGESAA
GGRK
//
