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Database: UniProt
Entry: D3GZW0_ECO44
LinkDB: D3GZW0_ECO44
Original site: D3GZW0_ECO44 
ID   D3GZW0_ECO44            Unreviewed;      1368 AA.
AC   D3GZW0;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   Name=ftsK {ECO:0000313|EMBL:CBG33806.1};
GN   OrderedLocusNames=EC042_0982 {ECO:0000313|EMBL:CBG33806.1};
OS   Escherichia coli O44:H18 (strain 042 / EAEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG33806.1, ECO:0000313|Proteomes:UP000001407};
RN   [1] {ECO:0000313|EMBL:CBG33806.1, ECO:0000313|Proteomes:UP000001407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX   PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA   Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA   Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA   Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA   Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT   "Complete genome sequence and comparative metabolic profiling of the
RT   prototypical enteroaggregative Escherichia coli strain 042.";
RL   PLoS ONE 5:E8801-E8801(2010).
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; FN554766; CBG33806.1; -; Genomic_DNA.
DR   RefSeq; WP_000077077.1; NC_017626.1.
DR   KEGG; elo:EC042_0982; -.
DR   PATRIC; fig|216592.3.peg.1013; -.
DR   HOGENOM; CLU_001981_0_1_6; -.
DR   Proteomes; UP000001407; 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: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:CBG33806.1};
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        25..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1013..1226
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          357..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1030..1037
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1368 AA;  151161 MW;  E5D0038A082E9FA1 CRC64;
     MSQEYTEDKE VTLTKLSSGR RLLEALLILI VLFAVWLMAA LLSFNPSDPS WSQTAWHEPI
     HNLGGMPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSSDEYIDYF AVSLRIIGVL
     ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIALLCV WAAGLTLFTG
     WSWVTIAEKL GGWILNILTF ASNRTRRDDT WVDEDEYEDD EEYEDENHGK QHESRRARIL
     RGALARRKRL AEKFINPMGR QTDAALFSGK RMDDDEEITY TARGVAADPD DVLFSGNRAT
     QPEYDEYDPL LNGAPITEPV AVAAAATTAT QSWAAPVEPV TQTPSVASVD VAPAQPTVAW
     QPVPGPQTGE PVIAPAPEGY PQQPQYAQPA VQYNEPLQQP VQPQQPYYAP AAEQPVQQPY
     YATAPEQSAQ QSYYAPAPEQ SVAGNAWQAE EQQSTFAPQS TYQTEQTYQQ PVAQEPLYQQ
     PQPVEQQPVV EPEPVVEETK PARPPLYYFE EVEEKRARER EQLAAWYQPI PEPVKEPEPI
     KSSLKAPSVA AVPPVEAAAA VSPLASGVKK ATLATGAAAT VAAPVFSLAN SGGPRPQVKE
     GIGPQLPRPK RIRVPTRREL ASYGIKLPSQ RAAEEKAREA QRNQYDSGDQ YNDDEIDAMQ
     QDELARQFAQ TQQQRYGEQY QHDVPVNAED ADAAAEAELA RQFAQTQQQR YSGEQPAGAN
     PFSLDDFEFS PMKALLDDGP HEPLFTPIVE PVQQPQQPVA PQQQYQQPQQ PVAPQQQYQQ
     PQQPVAPQQQ YQQPQQQVAP QPQYQQPQQP VAPQQQYQQP QQPVAPQQQY QQLQQPVAPQ
     PQYQQPQQPV APQPQDTLLH PLLMRNGDSR PLHKPTTPLP SLDLLTPPPS EVEPVDTFAL
     EQMARLVEAR LADFRIKADV VNYSPGPVIT RFELNLAPGV KAARISNLSR DLARSLSTVA
     VRVVEVIPGK PYVGLELPNK KRQTVYLREV LDNAKFRDNP SPLTVVLGKD IAGEPVVADL
     AKMPHLLVAG TTGSGKSVGV NAMILSMLYK AQPEDVRFIM IDPKMLELSV YEGIPHLLTE
     VVTDMKDAAN ALRWCVNEME RRYKLMSALG VRNLAGYNEK IAEADRMMRP IPDPYWKPGD
     SMDAQHPVLK KEPYIVVLVD EFADLMMTVG KKVEELIARL AQKARAAGIH LVLATQRPSV
     DVITGLIKAN IPTRIAFTVS SKIDSRTILD QAGAESLLGM GDMLYSGPNS TLPVRVHGAF
     VRDQEVHAVV QDWKARGRPQ YVDGITSDSE SEGGAGGFDG AEELDPLFDQ AVQFVTEKRK
     ASISGVQRQF RIGYNRAARI IEQMEAQGIV SEQGHNGNRE VLAPPPFD
//
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