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
//