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Database: UniProt
Entry: D9S7L9_FIBSS
LinkDB: D9S7L9_FIBSS
Original site: D9S7L9_FIBSS 
ID   D9S7L9_FIBSS            Unreviewed;      1032 AA.
AC   D9S7L9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:ADL25885.1};
GN   OrderedLocusNames=FSU_2996 {ECO:0000313|EMBL:ADL25885.1};
OS   Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL25885.1, ECO:0000313|Proteomes:UP000000517};
RN   [1] {ECO:0000313|Proteomes:UP000000517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517};
RA   Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA   Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT   "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; CP002158; ADL25885.1; -; Genomic_DNA.
DR   RefSeq; WP_014547050.1; NC_017448.1.
DR   AlphaFoldDB; D9S7L9; -.
DR   STRING; 59374.FSU_2996; -.
DR   GeneID; 34756781; -.
DR   KEGG; fsc:FSU_2996; -.
DR   PATRIC; fig|59374.8.peg.2867; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_6_2_0; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000000517; Chromosome.
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        35..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          676..876
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         693..700
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1032 AA;  111864 MW;  642D065954742C6A CRC64;
     MAAQKKKTVK KTKKPKVEPK AENQVPDSYF VTMMVGYFVM LAGIVLLLGC VTLSIAGAKG
     NWLGDYFGAM FPEFMTFLFG RVAVVVFTAA LVLWGLFIAI ASLRPKLLRF AVGASLLVVD
     LSFLMSLKNF GVRGVTNDAI SMNGGVLGQF FLQNLAIPVF GRTSYVAPLI LLLVALAMIL
     VLSFGVRPRH FRFIPQTMRY VCGVFGQRRS LGKVEIETLD FPDVNPEKKA AEKKTLRRGV
     VMEDETMIFV PDSVKMRRRG KVEPFNARHN WLTDDLDVNR SEMQTQVGDS FGLPQYAAGN
     VPGNAVPENV AANAPVANVA NASAGATLGG ADEDGAYEDP EIRRLEEELR LNERHMNALQ
     ILEIKERIGA LRRARDLIDW EKGHKGRMQV KGDVRRTAGS ETVGAAIAGN AGGNVSPKST
     KPMTVTTPRV AKPSGGEVKS STSANTIVCD ATLSDSVETR AAIHAEELLG GDGAYVEDFP
     GSPAVDDDET FAPVVVGADE VGEDPTFGSD FGGNARPASK PAVHSAPIPV APTASYDEYK
     IPEIAKILDT HEAQTADYTE EELNAIGKML EEKLENFKVK GRVIGCETGP MITRFEVEPG
     PGVKVSRFSA LQEDLALPLK VSSIRILAPI PGKAAVGVEI PNRKFQTVFC RDVFMSEKFK
     PAHDKILVAL GKDITGESFT MDLAKAPHLL IAGQTGSGKS VCINALMASM LFSKTPDELR
     MILVDPKAVE LKMYENIPHL LAPVITKPEI AIQALQWLCY EMDRRTEVLA SAKVRNIGGF
     NAKFEAGELP DEVPEEDRGH RMAFIVVIID EMADLMMVAG KEIEKSVARL AAKARAVGIH
     LVLATQRPSV KVITGIIKAN LPTRISFKVA SQIDARTVMD HAGAEKLLGR GDMLYKAVND
     PDPVRVHGAF LSDEEAERLA DACSDQNVFY PQVESFDVSG GEEGDEEGGG SLKNEKLDKL
     LFEVAQWAIS VNGLSTSAVQ RHFSVGYSRA GKIVDQLYGL GVCGPSKGNS KPRAMLIGMD
     ELMQLERSGR FG
//
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