FTSK_BRADU
ID FTSK_BRADU Reviewed; 825 AA.
AC Q89WR2;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=blr0616;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(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. Translocation stops specifically at Xer-dif sites, where FtsK
CC interacts with the Xer recombinase, allowing activation of chromosome
CC unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC the direction of DNA translocation. FtsK can remove proteins from DNA
CC as it translocates, but translocation stops specifically at XerCD-dif
CC site, thereby preventing removal of XerC and XerD from dif (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Located at the septum.
CC {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 multimerise to produce a hexameric ring,
CC contain the nucleotide binding motif and form the DNA pump. The gamma
CC subdomain is a regulatory subdomain that controls translocation of DNA
CC by recognition of KOPS motifs and interacts with XerD recombinase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; BA000040; BAC45881.1; -; Genomic_DNA.
DR RefSeq; NP_767256.1; NC_004463.1.
DR RefSeq; WP_011083444.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89WR2; -.
DR SMR; Q89WR2; -.
DR STRING; 224911.27348865; -.
DR PRIDE; Q89WR2; -.
DR EnsemblBacteria; BAC45881; BAC45881; BAC45881.
DR GeneID; 64020478; -.
DR KEGG; bja:blr0616; -.
DR PATRIC; fig|224911.44.peg.9156; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_6_1_5; -.
DR InParanoid; Q89WR2; -.
DR OMA; IGPANHA; -.
DR PhylomeDB; Q89WR2; -.
DR Proteomes; UP000002526; 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 inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..825
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098242"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..825
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 457..676
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 254..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477..482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 825 AA; 89035 MW; 96F7C679D932B7F7 CRC64;
MSMSAIERVI PLVGHLPPSI REGLARRMRE LAGLGLIALS GLASAALMTW SVQDASLSHA
TSRPIRNILG YAGAIGADLA MQILGLGAIM LVLTVAVWGW RMMTHRPFDR EALRLGSWIL
CTVIAAGFVS CWPHGGAWPL PTGLGGVVGD ALVRAPAVIF GPPGMIYRTV LGVILFAAMA
ATFLIACGLG AREHDDELAE IEDDDKPLDE DEESDRGSVS LGWLFHALMS TKARLIWLCG
AAYRSLVSSG PKTRAVGFSR QEPNLGGGRA APPISPRSED EDYEEEHEEE EDEEEEEEPA
ARAPRKKAAP KAAAKKSSDK FELPSVSVLA APKAGDRQPL SKAELEANSR ALEGVLQDFG
VRGEIVKANP GPVVTLYELE PAPGIKSSRV IGLADDIARS MSALSARVAV VPGRNAIGIE
LPNAHREKVY LRELLVAKET VDTVAKLPLC LGKTIGGDPV IIDLARTPHM LIAGTTGSGK
SVAINTMILS LVYRLRPDQC RLIMVDPKML ELSVYDGIPH LLTPVVTDPK KAVVALKWAV
REMEERYKNM AKLGVRNIDG YNTRLLELKA KGEEPTRTVH TGFDKETGKA IYEEEKLSLD
PLPYIVIIVD EMADLMMVAG KDIEGAVQRL AQMARAAGLH VILATQRPSV DVITGTIKAN
FPTRIAFQVT SKIDSRTILG EMGAEQLLGQ GDMLYMAGGG RISRVHGPFA SDDEVEKVVR
HLKTQGQPEY LEAVTAEEPT EDEDGGAVFD ASGMGADGGG DLFQQAVAIV KRDRKASTSY
IQRRLQIGYN RAASLMERME LEGIVGPANH AGKREILVEE EDSHM
