ID A0A1I6P0M0_9CAUL Unreviewed; 797 AA.
AC A0A1I6P0M0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=SAMN05192570_0721 {ECO:0000313|EMBL:SFS33739.1};
OS Brevundimonas viscosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=871741 {ECO:0000313|EMBL:SFS33739.1, ECO:0000313|Proteomes:UP000198788};
RN [1] {ECO:0000313|Proteomes:UP000198788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10683 {ECO:0000313|Proteomes:UP000198788};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOZV01000001; SFS33739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6P0M0; -.
DR STRING; 871741.SAMN05192570_0721; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000198788; Unassembled WGS sequence.
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};
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 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 436..654
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 206..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..266
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 453..460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 797 AA; 85493 MW; A23BF8A7AD69D6CD CRC64;
MSAALVLGQR AWIGARILWD APFVVRFRGV LQALLAALLL VALLSWNPAD PSLNAASTAA
PTNWLGANGA LFADLFMQSL GLAAWPGALL LVAFGLARAI GDAIQQRLKP TPVKALSATG
GVLALSAALS ALAPPAAWPL AAGLGGLWGD ALVGLVRWAC EALRFGGGSI IAGVLFLPLA
LWGIGYAIGL RFSDLSEALA WSGSRRAAPR RAEAAPAAAP RPRRPRPEPE PEPEPEPGHA
PVNLAPEPEE MPPWDEPAPA PRPARAAPEP RVAAVKAPKA SRREVDDAQA AFDFARPEGD
FDLPPLGMLS KPAKRVAAVD EEALKQNAKM LEGVLQEFGV RGVIDQIRPG PVVTLYELVP
APGVKHGRVV ALSDDIARSM SARACRISVV QGRNAIGIEL PNARRETVYL RDLLASTEYD
KPSHLLPLAL GETIGGEPYV ADLARMPHLL IAGTTGSGKS VGVNAMILSI LYKLTPEQCR
FIMIDPKMLE LSVYDGIPHL LAPVVTDPKK AVVALKWTVR EMEDRYRRMS KLGVRNIASY
NDRAREAQAK GEHFERTVQT GFDEQGRPVY ESEKIRPEPM PYLVVVMDEM ADLMLVAGKD
VEGAVQRLAQ MARAAGIHLI MATQRPSVDV ITGTIKANFP TRISFQVTSK IDSRTILGEQ
GGEQLLGQGD MLYMAGGGRI TRLHGPFVDD KEVEAVCNHL KAQAEPDYLD LITDDPDGDG
DNAFGDEGGG SGDDLYDRAV AVVTRDRKAS TSYIQRRLQI GYNRAASLIE RMEQEGVVSP
ANHAGKRDIL AGPPPMV
//
