ID A0A0S2W576_9FIRM Unreviewed; 898 AA.
AC A0A0S2W576;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:ALP94431.1};
GN ORFNames=IB211_02040c {ECO:0000313|EMBL:ALP94431.1};
OS Intestinimonas butyriciproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Intestinimonas.
OX NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP94431.1, ECO:0000313|Proteomes:UP000064844};
RN [1] {ECO:0000313|EMBL:ALP94431.1, ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|EMBL:ALP94431.1,
RC ECO:0000313|Proteomes:UP000064844};
RX PubMed=26620920; DOI=10.1038/ncomms10062;
RA Bui T.P., Ritari J., Boeren S., de Waard P., Plugge C.M., de Vos W.M.;
RT "Production of butyrate from lysine and the Amadori product fructoselysine
RT by a human gut commensal.";
RL Nat. Commun. 6:10062-10062(2015).
RN [2] {ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT "A butyrogenic pathway from the amino acid lysine in a human gut
RT commensal.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011307; ALP94431.1; -; Genomic_DNA.
DR RefSeq; WP_058117950.1; NZ_JADMQW010000035.1.
DR AlphaFoldDB; A0A0S2W576; -.
DR STRING; 1297617.IB211_02040c; -.
DR KEGG; ibu:IB211_02040c; -.
DR PATRIC; fig|1297617.4.peg.2104; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000064844; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; 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; 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; 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:0000313|EMBL:ALP94431.1};
KW Cell division {ECO:0000313|EMBL:ALP94431.1};
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000064844};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 513..704
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 530..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 898 AA; 97103 MW; 0590A6F0DBEA283F CRC64;
MASTQKKNTG GKRAASSSGK RTSGATARKG SGGRRSSAAP QPKPIRREVG AVVCLLLAFF
AAFGYFNIKA LFIDLFCSLL KGLFGYGFWL APPMLAVASY ILAFHRGRPV RLRLWCALLT
PLVMGAILHL FLYKGEFAMG LEGIQGLWTQ GLEVKCGGVV SGLIAETLVL VFSRVGGGVI
LILGQCLMFL GAFHLSVVDI VDAFRNRPRP AYEYEEEEET PEPKPARRKP VPVEERRRAA
IDIPVDDGPV PPPERHPERP FTPQKERFFN RKAGVLPPDQ VLTGGKPMDA KAPEAVPETQ
SPASEEAGIE VQPIPVPEPA AAEPPAPVQA EPEVPPMPEI EREPAVEKVT PKEARAAAAE
VSRDIEKGMV EAVPAAYQYP PVSLLTEGGG EVGTSAQNEL KMNQERLSDT IRSFGIEARI
SDVTRGPSVT RYEVELDQGV RLNKLTNLAD DIALALGATG VRIAPIPDKI ATVGIEVPNK
LVSPVHIHEV IDSKAFRDHA SKVAFAVGKD IGGNCIVGNI AKLPHLLIAG TTGSGKSVCT
NSLIISLLYK ATPEEVRLIM VDPKMVELGI YNGIPHLLIP VVTDPKKAAG ALQWAVSEMM
KRYRAFSEVG VRDLASYNVH AAKTEGMEKM PQVVVVIDEL ADLMLVAAKE VEESICRVAQ
MGRAAGMHLI IATQRPSADV ITGLMKANIP SRIAFAVASA LESRIILDTT GAEKLVGRGD
MLYFPLGSGK PLRVQGCLIS DEEVASVVEF IKRQSTAEYD EEVIHEIEQH AAEKDKQGKG
VGGSAPEEVG NDYDELLPAA IEVVVETGQA SVSMLQRRLK LGYSRAARLV DQMEEKGIVG
PFEGSKPRQL LITKEQWQEM QFKQGLVDAA PEPVPDELEF EGDAVPQSRE LPPFDLED
//
