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Database: UniProt
Entry: A0A0W0YQ93_9GAMM
LinkDB: A0A0W0YQ93_9GAMM
Original site: A0A0W0YQ93_9GAMM 
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}.
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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
//
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