ID A0A2A2EHP0_9BIFI Unreviewed; 496 AA.
AC A0A2A2EHP0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:PAU68507.1};
DE Flags: Fragment;
GN ORFNames=B1400_1429 {ECO:0000313|EMBL:PAU68507.1};
OS Bifidobacterium italicum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1960968 {ECO:0000313|EMBL:PAU68507.1, ECO:0000313|Proteomes:UP000217986};
RN [1] {ECO:0000313|EMBL:PAU68507.1, ECO:0000313|Proteomes:UP000217986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70 {ECO:0000313|EMBL:PAU68507.1,
RC ECO:0000313|Proteomes:UP000217986};
RX PubMed=28837128; DOI=10.1038/ismej.2017.138;
RA Milani C., Mangifesta M., Mancabelli L., Lugli G.A., James K., Duranti S.,
RA Turroni F., Ferrario C., Ossiprandi M.C., van Sinderen D., Ventura M.;
RT "Unveiling bifidobacterial biogeography across the mammalian branch of the
RT tree of life.";
RL ISME J. 11:2834-2847(2017).
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 -!- 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:PAU68507.1}.
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DR EMBL; MVOG01000029; PAU68507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2EHP0; -.
DR Proteomes; UP000217986; Unassembled WGS sequence.
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:PAU68507.1};
KW Cell division {ECO:0000313|EMBL:PAU68507.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 121..321
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 138..145
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:PAU68507.1"
SQ SEQUENCE 496 AA; 53566 MW; 17F008859E993DE0 CRC64;
HAAHTQANDN VIRALDTTFQ QFKVDAKVVG FLRGPSVTQY EVEVAPGVKV EKVTNLDKNI
AYAVASSDVR ILSPIPGKSA IGIEIPNTDR EIVHLGDVLR SDKAMNDPNP MLAGVGKDVE
GHFVTADLTK MPHLLVAGAT GSGKSSFINS MLTSIIMRAT PDQVRMIMVD PKRVELSAYA
GIPHLLTPII TDPKKAAQAL EWVVKEMDAR YSDLEFFGFR HVKDFNEAVR AGKVHAPAGS
KRKVAPYPYL LVVVDEMADL MMVAKNDVES SIQRITQLAR AAGVHLVLAT QRPSVDVVTG
LIKANIPSRL AFATSSATDS RVILDATGAE TLIGQGDALF MPMGMAKPIR VQGAWVNESE
IRKAVDFVRQ QRKPHYRPDI EQMANEAEKS KLDPTEDIGG DMDELLQAAE LVVSSQFGST
SMLQRKLRVG FAKAGRLMDL LESRGVVGPS EGSKAREVLV QPADLPQVLA FIKGETTSLT
AASEAPPQAP PQPSGD
//
