ID A0A086ZG55_9BIFI Unreviewed; 838 AA.
AC A0A086ZG55;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:KFI45505.1};
GN ORFNames=BBOH_1086 {ECO:0000313|EMBL:KFI45505.1};
OS Bifidobacterium bohemicum DSM 22767.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437606 {ECO:0000313|EMBL:KFI45505.1, ECO:0000313|Proteomes:UP000029096};
RN [1] {ECO:0000313|EMBL:KFI45505.1, ECO:0000313|Proteomes:UP000029096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22767 {ECO:0000313|EMBL:KFI45505.1,
RC ECO:0000313|Proteomes:UP000029096};
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 -!- 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:KFI45505.1}.
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DR EMBL; JGYP01000002; KFI45505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086ZG55; -.
DR STRING; 1437606.BBOH_1086; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000029096; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000029096};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 464..664
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 108..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 481..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 838 AA; 89615 MW; 482AB474A07B6E77 CRC64;
MSVLRIVGGV ALVLVCICSV TDSFAVSIHM PFSMDALRGA GGLVGYVPGT LLARGLSPVF
AALLDVVLTF FLLILMMGFA RFKRLCAPLL DAVSNWFDGH MRTRQEADDV AAASEHEQFP
DEAGVGGDTL DFAEGVPMHE DGDSGQRRTS RVADIDRPKN KGIGAFFSRL FGRSGKNRAD
ADIDRYAGDE PFDHAAATEK TDPLSYGSDD RLRTVVDPVT GEVFSVHAAD AFPSNVADAG
ATQVLPVVAP TGADGAYVAP SESQTNGSQA DPWAVVNSDG AMSGDGAMPA EEIVKGVAGG
AANLPASVAN TGTGDDTGEP VEDDEPAGPY QLPDLDMLVK GKPHMARTKA NDNVIQALTD
TFKEFGVDAK VIGFLRGPSV TQYEVELGPG VKVEKVTNLQ RNIAYAVAST DVRILSPIPG
KSAIGIEIPN IDREIVHLGD VLRSDKAMND PNPMLAGVGK DVEGHFVTAD LTKMPHLLVA
GATGSGKSSF INSMLTSIIM RATPEQVRLI MVDPKRVELS AYAGIPHLLT PIITDPKKAA
QALEWVVKEM DARYDDLQYF GFRHIKDFNK AVREGKVHPP LGSKRKVAPY PYILVVVDEM
ADLMMLAKND VESSIQRITQ LARAAGVHLV LATQRPSVDV ITGLIKANIP SRLAFATSSA
TDSRVILDTT GAESLIGQGD ALFLPMGSAK PIRVQGSWVG ESEIRQAVRF ARTQRKPHYR
DDIAQMAEQA EQNQAHPDEE IGDDMDTLLE AAKLVVTTQF GSTSMLQRKL RIGFAKAGRM
MDLLESRGVV GPSEGSKARE VLVQPQDLTQ TLDFIQGKTS SIVPSDAVAE QADPADET
//
