ID A0A159Z8K2_9RHOB Unreviewed; 1052 AA.
AC A0A159Z8K2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=AKL17_4655 {ECO:0000313|EMBL:AMY71865.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY71865.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY71865.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) 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. 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.
CC {ECO:0000256|ARBA:ARBA00024784}.
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}.
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DR EMBL; CP012661; AMY71865.1; -; Genomic_DNA.
DR RefSeq; WP_066817631.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A159Z8K2; -.
DR STRING; 1335048.AKL17_4655; -.
DR KEGG; daa:AKL17_4655; -.
DR PATRIC; fig|1335048.3.peg.4832; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000076128; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; 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, ECO:0000313|EMBL:AMY71865.1};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 689..908
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 443..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 706..713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1052 AA; 113927 MW; A525AA26B24D5C3C CRC64;
MASYQARQRD PLLDQNMQAA LERRGKELLG AALVVLGVMT AMMLASYSPD DPSFLAATNE
PAMNLLGRFG AAIASPLYVI AGHGAWGIAI AFIAWGLRFI THRGEERALG RVIFVPIGVA
LMSVYASTLM PGPLWTHSFG LGGLFGDTIL GALIGVAPVK ATFGLKLISL LVGAGVVIVG
AFVTGFDRAE TRAVVRFLLI GAVLVYTRLL MLAGRGAEAS VRAAQVAAEK ARERRALARD
RAAEAAAWAE AERSVPAPQP SRRVMRADPR YVAVAEEDER LVEEEPATWT PAPQKQGLLA
RMPAMIRRAV EPDPEPELVE PRVARGAWNA EAPSEDRIRA RIVDAVKTRQ IVAEQRYPAP
QPQPVAQAQP RRAEPPVTAA ALAAAAARQA SAAAGPLFAA SRARMPEATP APMLKAEPRF
MPQVRMQAAP PSAPALRPVE PPLTARPASR PLSAAAPLHD SVPSEMYDSN LDELDRIDPA
LAHDRFDDED FDRNAFAEIY DDEAEAAWTP PPAAGPRKVV LHHLPKKTVA PSRQARAEAQ
PRLRFEEPAP VVYEAPPLSL LTNPASIQRH SLADEALEEN ARMLENVLDD YGVKGEIVSV
RPGPVVTMYE LEPAPGLKAS RVIGLADDIA RSMSALSARV STVPGRTVIG IELPNAFREK
VVLREILSAR DFGDSNMRLP LALGKDISGE PVVANLAKMP HLLIAGTTGS GKSVAINTMI
LSLLYKLSPE ECRLIMIDPK MLELSVYDGI PHLLSPVVTD PKKAVVALKW VVGEMEERYR
KMSKMGVRNI EGYNGRVREA LDRGEMFKRT VQTGFDEETG DPIFETDEFQ PKTIPYIVVV
VDEMADLMMV AGKEIEACIQ RLAQMARASG IHLIMATQRP SVDVITGTIK ANFPTRISFQ
VTSKIDSRTI LGEQGAEQLL GMGDMLYMAG GSRITRIHGP FVSDEEVEEI VTHLKSYGPP
EYMSGVVEGP DEDKEADIDA VLGLGGGEGE DALYDSAVAV VLKDRKVSTS YIQRKLGIGY
NKAARLVEQM EEEGLVSAAN HVGKREILVP EQ
//
