ID R0ELM3_CAUVI Unreviewed; 819 AA.
AC R0ELM3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=OR37_01387 {ECO:0000313|EMBL:ENZ82809.1};
OS Caulobacter vibrioides OR37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ82809.1, ECO:0000313|Proteomes:UP000013063};
RN [1] {ECO:0000313|EMBL:ENZ82809.1, ECO:0000313|Proteomes:UP000013063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR37 {ECO:0000313|EMBL:ENZ82809.1,
RC ECO:0000313|Proteomes:UP000013063};
RX PubMed=23792749;
RA Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA Palumbo A.V., Brown S.D.;
RT "Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
RT Tolerant to Heavy Metals.";
RL Genome Announc. 1:0-0(2013).
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}.
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:ENZ82809.1}.
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DR EMBL; APMP01000005; ENZ82809.1; -; Genomic_DNA.
DR AlphaFoldDB; R0ELM3; -.
DR STRING; 1292034.OR37_01387; -.
DR PATRIC; fig|1292034.3.peg.1375; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000013063; 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 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 456..674
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 211..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 819 AA; 87953 MW; 81995259DFB20E48 CRC64;
MARAARRSTA EFLWDAIRYS WIQPWTARFR GGVVTVVGAG LLLAIATYNA TDPSFNAVTG
EPARNALGGL GAAVADLLMQ SLGLSAWGVA LLMLVFGVTR VAQADPDMER KHLRQRAVVG
ALGLLALSAT LAAPPPPAIW QLEKGLGGFW GDGLLRMVAG VLHFAHIPGA TIIAAILFAV
AAIAALGFAF GVRDVDPDAI HAAVANALQP RVRAEPEPPP VAKPARAKRE KAEAAPRRER
PGRLPPIDEE DAAPVASAPA RAAPERAYTP PAADQDDEDA FEDMLDARPM AIAKPKAPPK
ESGREQREQQ KAFAFEDEGG FQLPELAMLA KSKPRSSEVD AGALRQNARL LESVLAEFGV
KGQIDQIRPG PVVTMYELVP APGVKTARVV ALADDIARSM SVISCRVAVA QGRNAIGIEM
PNSKRETVYL RDLLSSADYE KASQILPMAL GETIGGEPYI ADLAKMPHLL IAGTTGSGKS
VGVNAMILSI LYKLPPEKCR FIMVDPKMLE LSVYDGIPHL LAPVVTDPKK AVVALKWTVR
EMEDRYRRMS KIGVRNIGGY NEKANEAAAK GEHFERTVQT GFDDAGRPIY ETEQIRPEPM
PYLVVVIDEV ADLMMVAGKD IEGAVQRLAQ MARAAGIHLI MATQRPSVDV ITGTIKANFP
TRISFQVTSK IDARTILGEQ GAEQLLGQGD MLYMAGGGRI TRLHGPFVSD GEVEAVAKFL
RDQGIPQYLE EVTAGGDEEQ EEAIEGAFSG EGGANDLYDH AVAVVTRDRK ASTSYIQRRL
QIGYNRAASL MERMEKEGVV GAANHAGKRE ILAPPPPPL
//
