ID A0A1Y4WJZ1_9FIRM Unreviewed; 883 AA.
AC A0A1Y4WJZ1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:OUQ81913.1};
GN ORFNames=B5E42_10150 {ECO:0000313|EMBL:OUQ81913.1};
OS Flavonifractor sp. An10.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Flavonifractor.
OX NCBI_TaxID=1965537 {ECO:0000313|EMBL:OUQ81913.1, ECO:0000313|Proteomes:UP000196537};
RN [1] {ECO:0000313|Proteomes:UP000196537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An10 {ECO:0000313|Proteomes:UP000196537};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUQ81913.1}.
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DR EMBL; NFMB01000005; OUQ81913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4WJZ1; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000196537; 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 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; 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}; Cell cycle {ECO:0000313|EMBL:OUQ81913.1};
KW Cell division {ECO:0000313|EMBL:OUQ81913.1};
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:UP000196537};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 498..689
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 515..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 883 AA; 94815 MW; F1E3C509C7B5DD64 CRC64;
MATTQKKTTG GSRAASGRSG TASRSGGSRK KAPAPRPIRR EVGAVVCLLL AIFSAFGYFH
IQAIFIDFFC GLVKGLIGYG YWLLPPMLLV ASGILLFHRG RPVRLRVWCA LLTPVLAGGL
LHLILAKGPY EWNAALVKTL WTQGEALQSG GVVSGAAALG LSAVFSPIGA GIILVLVALI
LLMAAFHISP VELVDKLRAR TWAEYEEEEL PEPRPRERRR KEPEASAPAA EAQSAAQRRQ
TPQIDIPVDE GPLVGKKVEP PPVEKKERFF NRKPSVPAPD QVLAGEEGLE PPAEAAEEPE
APDAPAPAAE APVPEPAPVP PMPEIQREPA VGKVKKEEAA QAAAEVAQDI ARNLEEGLPA
AYQYPPVSLL HEGQGVSGSE VAGELQANQA RLADTIHSFG IDAEIVSVTR GPSVTRYEVE
LDQGVRLNKL TNLSDDIALA LGATGVRIAP IPDKISMVGI EVPNKLVSPV PIHDVIDSKE
FRDNPSKVAF AVGRDISNRN VVGNIAKLPH LLIAGTTGSG KSVCTNSLII SLLYKATPEE
VRLIMVDPKM VELGIYNGIP HLLIPVVTDP KKAAGALQWA VVEMMKRYRT FSEIGVRDLA
SYNAHAARSD ELEKMPQIVI VIDELADLML VAAKEVEESI CRVAQMGRAA GMHLIIATQR
PSADVITGLM KANIPSRIAF AVASSLESRI ILDTTGAEKL VGRGDMLYFP LGTGKPQRVQ
GCLISDEEVA AVVGFIKQNS GAAQYDQEII HDIEQHAAEK DKGAKGVGGS APEEVGEEYD
ELLPSAIEVV VETGMASVSM LQRRLKLGYS RAARLVDQME EKGVVGPFEG SKPRQVLITK
EQWQEMQFKQ GMVDAAPAEP VPDELPFEGD AVPQERDSPP FDL
//
