ID A0A0W0YQ93_9GAMM Unreviewed; 811 AA.
AC A0A0W0YQ93;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN Name=ftsK {ECO:0000313|EMBL:KTD59019.1};
GN ORFNames=Lsha_2051 {ECO:0000313|EMBL:KTD59019.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD59019.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD59019.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD59019.1,
RC ECO:0000313|Proteomes:UP000054600};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD59019.1}.
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; LNYW01000052; KTD59019.1; -; Genomic_DNA.
DR RefSeq; WP_018576627.1; NZ_LNYW01000052.1.
DR AlphaFoldDB; A0A0W0YQ93; -.
DR STRING; 1122169.Lsha_2051; -.
DR PATRIC; fig|1122169.6.peg.2345; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000054600; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; 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:KTD59019.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
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}; Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 454..667
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 285..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 471..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 811 AA; 88482 MW; 69EAE0578ED84463 CRC64;
MAKQDAGKQA ATPKKNLPNF IVKRLSEGSF ILILSGALFM LLSLFTYKMS DPGWSHASRS
GVDIANSGGT VGAYLADALY FAFGYFAYLL PLAVVYVAWA ILKDFHSLKA IDKPVLILRS
VGFILMICGG CGLLSLEPQI QPIDAIHSAG GIIGQTVSSG WYQMLNLHGA TIILFAMLLV
GITWLTGLSW VKATELIGFY TLFAFNAAYS SVRKMLHLSN AGIERYKARE PASNPVEKQE
KQEKRQIQEK VISKLFGSKK AKEREPEQER KLPVLIASAE TKPESVKPVE KVKEVREPRD
NPQTREIRAP KMNASGSLPG LDLLDKGQPG KPMGGYTHQE LENVSRDVEQ HLLDFGIQAD
VVAVHPGPVV TRFELQLAAG VKVSKLSALS KDLARSLSVI SVRVVEVIPG KTVVGLELPN
HSREIVRLSD VLSADVYQQA HSPLTLALGV DIAGHPMVVD LAKMPHLLVA GTTGSGKSVG
INAMILSILF KATPEQVRLI MVDPKMLELS VYDGIPHLLT PVVTDMKEAA SALRWCVEEM
ERRYKLMASL GVRNLAGYNT KIAEGIASGE PLVNPLWKPV DSMDEAAPQL EALPYVVVVI
DELADMMMVV GKKVEQLIAR IAQKARAAGI HMILATQRPS VDVLTGLIKS NIPTRMSFQV
SSKIDSRTIL DQQGAEQLLG HGDMLYLAPG SGAPLRVHGA FVDDKEVHRI ADDWRARGEP
DYIDDIIKMT GDGEGGTDEE GQATEDDDPL YDQAVEFVVQ TRKASISAVQ RRLKIGYNRA
ARIIEEMERT GIVGPLDGGY RDVLVTSITE D
//