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Database: UniProt
Entry: A0A087B3P0_9BIFI
LinkDB: A0A087B3P0_9BIFI
Original site: A0A087B3P0_9BIFI 
ID   A0A087B3P0_9BIFI        Unreviewed;       958 AA.
AC   A0A087B3P0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:KFI65640.1};
GN   ORFNames=BCUN_0135 {ECO:0000313|EMBL:KFI65640.1};
OS   Bifidobacterium cuniculi.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI65640.1, ECO:0000313|Proteomes:UP000029067};
RN   [1] {ECO:0000313|EMBL:KFI65640.1, ECO:0000313|Proteomes:UP000029067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI65640.1,
RC   ECO:0000313|Proteomes:UP000029067};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential cell division protein that coordinates cell
CC       division and chromosome segregation. The N-terminus is involved in
CC       assembly of the cell-division machinery. The C-terminus functions as a
CC       DNA motor that moves dsDNA in an ATP-dependent manner towards the dif
CC       recombination site, which is located within the replication terminus
CC       region. Required for activation of the Xer recombinase, allowing
CC       activation of chromosome unlinking by recombination.
CC       {ECO:0000256|ARBA:ARBA00024986}.
CC   -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC       {ECO:0000256|ARBA:ARBA00025923}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KFI65640.1}.
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DR   EMBL; JGYV01000001; KFI65640.1; -; Genomic_DNA.
DR   RefSeq; WP_051920396.1; NZ_JGYV01000001.1.
DR   AlphaFoldDB; A0A087B3P0; -.
DR   STRING; 1688.BCUN_0135; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000029067; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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:0007049; P:cell cycle; 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; IPR025199; FtsK_4TM.
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; PF13491; FtsK_4TM; 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:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000029067};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        70..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          582..782
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          228..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          937..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         599..606
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   958 AA;  101624 MW;  189EB4039FA81842 CRC64;
     MARSSSSQSS KPRKAQSGSS TSSQPKSRTA RPAQAEPWWQ RALLAVPRAL GSTVRKVSVG
     EYDPAYRRDG LCFVMLVLAV FFIGSEWFRV DGPLGRGLHA LAAGLFGVMS VVVPVLLAIV
     ALRLMRNSGK ESDNTRVIAG WALLLWAVCS IIDVIVASDV KGFSWENLRR AGGLFGFIVG
     SPLAWGLSQA FAVVVFVIAA LFALLLITRT HVTEVPDKLR QLFASDAADD NGHRGQEDPA
     AAGDDGLQFA QGVPAHDGSD DDSQDAPKRK EGFFARLFHR SRKATTDTHL DEYVGDEAFL
     NAASRHGDVA ETMVVADGAR SVSSGGAYDD DATRSIDSST WRAQEEAGHT VPMPSGSMPA
     VDPWSRLDGD GESMLVSRET GEVLTPPRTV QSVAATPSGV ASAAASHTAA GPSAAAAAPA
     TSAGASGAPM TAAEASAAAA AAVADRPYRL PSLDLLAQGK PHAQRTPANE RAIRALNNTF
     EQFKVDAKVV GFLRGPSVTQ YEVELAPGVK VSKLTGLQDD IKYALGSSTV RMLTPIPGKS
     AIGIELPNED REIVQLGDVL RSEKVMADHN PMLAGVGKDV EGHVVTADLT KMPHLLVAGA
     TGAGKSSFIN SMLTSIIMRA TPEQVRMIMV DPKRVELSMY AGIPHLITPI ITDPKKAASA
     LEWVVKEMDA RYSDLEFFGF RNVKDFNAAV RAGKVHAPAG SQRKVAPYPY LLVVVDEMAD
     LMMVAKNDVE GSIQRITQLA RAAGVHLVLA TQRPSVDVIT GLIKANIPSR LAFTTSSATD
     SRVILDATGA ETLIGQGDAL FLPMGSAKPV RVQGSWVGES EIRRAVEFAS AQRKPHYRED
     IEQMASEGEQ KKIDPTEDIG DDMDELLQAA ELVVSSQFGS TSMLQRKLRV GFAKAGRLMD
     LLESRGVVGP SEGSKAREVL VQPAELPQVL AFIKGDAPSI GSPAADGRPA VDDAGEAA
//
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