FTSK_BIFLO
ID FTSK_BIFLO Reviewed; 969 AA.
AC Q8G4H3;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=BL1411;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Located at the septum. {ECO:0000250}.
CC -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for the
CC localization to the septal ring and is required for cell division,
CC followed by a linker domain, and a C-terminal domain, which forms the
CC translocation motor involved in chromosome segregation. The C-terminal
CC domain can be further subdivided into alpha, beta and gamma subdomains.
CC The alpha and beta subdomains form the DNA pump, and the gamma
CC subdomain is a regulatory subdomain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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; AE014295; AAN25210.1; -; Genomic_DNA.
DR RefSeq; NP_696574.1; NC_004307.2.
DR RefSeq; WP_007052638.1; NC_004307.2.
DR AlphaFoldDB; Q8G4H3; -.
DR SMR; Q8G4H3; -.
DR STRING; 206672.BL1411; -.
DR EnsemblBacteria; AAN25210; AAN25210; BL1411.
DR GeneID; 66505429; -.
DR KEGG; blo:BL1411; -.
DR PATRIC; fig|206672.9.peg.269; -.
DR HOGENOM; CLU_001981_2_0_11; -.
DR OMA; IPNVDRE; -.
DR PhylomeDB; Q8G4H3; -.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..969
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098240"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..969
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 598..798
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 618..623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 969 AA; 102651 MW; 50711A08044CB794 CRC64;
MARTASSNST KPRKSKDNGS THDGETKVQP ELDLEPEPLW KKILLAIPRA FGSGVRAVTG
VGEYDPAYRR DGLCFLLLVL AVLFCASEWF RVSGPFGQLL HAIAAGVLGL MSVVLPVLLA
AVAFRLMRNS GKGSNNPRVV TGWVLLMWSI CSIIDVAIAA DHTGFDITIL QSAGGLFGFF
LGSPLAWGLS NVFAIIIFVV VGLFSLLMIT GTHVTDLPED ARKIAAKIQR KPYVPMGQET
DGSASQFPNE VRVGDTTLAF ADGVPSHDGD DDGSDNDQAG DARPSLFARL FGRKSKTEDD
KTLDKYAADD PFDRAASQHG ATAETPVVDP MTGEIIGART IASSSYDGRP HLSSPAPAAD
ADDGDASRTR VITSGQTVAM PGGGAVDDPW APSAAQAGTV ALAGAAGAMG AAGAAGAAAA
AAATGAYAGA DADGSGVGQG VPNTGGQPNA TAGNDTDDDA NRPYQLPDLN LLTKGQPHAM
RTPANDRVIR ALTSTFEQFN VDAKVVGFLR GPSVTQYEVE LGPGVKVEKV TNLQRNIAYA
VASSDVRILS PIPGKSAIGI EIPNEDREIV HLGDVLRSDK AVGDPNPMLS GIGKDVEGHF
VTADLTKMPH LLVAGATGSG KSSFINSMLT SIIMRATPEQ VRLIMVDPKR VELSAYAGIP
HLLTPIITDP KKAAQALEWV VKEMDARYSD LEFFGFRHVK DFNEAVRAGK VHAPAGSQRK
VAPYPYILVV VDEMADLMMV AKNDVESSIQ RITQLARAAG VHLVLATQRP SVDVVTGLIK
ANIPSRLAFA TSSATDSRVI LDTVGAETLI GQGDALFLPM GSAKPIRVQG SWVSESEIRK
AVEFVRTQRK PKYREDIEQM AKEAEKKDSM EPDEEIGDDM DVLLQAAELV VTSQFGSTSM
LQRKLRVGFA KAGRLMDLLE SRGVVGPSEG SKAREVLVQP QDLPQVLAFI RGETSSLEAT
APQQPELGE
