ID K2FS38_9BACT Unreviewed; 696 AA.
AC K2FS38;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 08-NOV-2023, entry version 45.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
DE Flags: Fragment;
GN ORFNames=ACD_7C00524G0001 {ECO:0000313|EMBL:EKE20569.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE20569.1};
RN [1] {ECO:0000313|EMBL:EKE20569.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKE20569.1}.
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DR EMBL; AMFJ01002763; EKE20569.1; -; Genomic_DNA.
DR AlphaFoldDB; K2FS38; -.
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 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 304..510
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 654..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..107
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 675..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 321..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKE20569.1"
SQ SEQUENCE 696 AA; 77012 MW; FE259B5E6807F4CA CRC64;
FFHIFYEYNI LAEVAKNGQG GGYIGYFIAW SLIKLTGKIV GIIFLVAFFS IGVMIAFNFS
LVEFFINLFK KKEIEEAAIK KDYENIIDNE KNNLEKEEAE NIGITELIDE ADLGCNIKEV
KFVEGPSAAE IDEEEIIGNK EKGFNIKSTS FESKIKNIKT NKASQISAGP WKLPSLTLLD
ESTGEAYSGN IDENTDIIKD TFSNFGIALE DGGVKIGPAV TQYSFRPAVG VKLSKIVALG
DDLALALAAH PIRIEAPIPG KSLIGIEVPN KKSIMIRLKN ALESEEFKSS KSPLTLALGK
NVEGNFVVAD LGKMPHLLIA GATGTGKSVC INSIILSLLF QNSPDDLKMI LVDPKRVELS
LYNKIPHLLS PVITDNKKVV NSLKWAVREM EERYKILEAV GSRDLESYSQ KFKKGMTRDV
IDPDTSEVVK EELKKLPFIV IVIDELADLM VSHGKDVEGA IMRLAQMARA VGIHLIISTQ
RPSVEVLTGI IKANITTRIA LQVASQIDSR TIIDMRGAEN LLGKGDLLFL SSESPKPRRL
QNSFVSENEV KRVVEYIIDQ ADRVYKKDED DDIEEELLGD ANGKNIAAGN NFGQVDFSIP
QDNEDEDVIY DEVKEFVLKL GKASASLLQR RFRIGYNRAA RLIDSLENDG IVGGADGSKP
REVLPGGNIS NRNKEAVDNN KDTEDITQEQ REKWQI
//
