ID C9Y055_CROTZ Unreviewed; 1338 AA.
AC C9Y055;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN Name=ftsK {ECO:0000313|EMBL:CBA29614.1};
GN OrderedLocusNames=Ctu_15020 {ECO:0000313|EMBL:CBA29614.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA29614.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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; FN543093; CBA29614.1; -; Genomic_DNA.
DR KEGG; ctu:CTU_15020; -.
DR PATRIC; fig|693216.3.peg.1431; -.
DR HOGENOM; CLU_001981_0_1_6; -.
DR Proteomes; UP000002069; 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};
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 55..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 983..1196
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 188..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..761
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1000..1007
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1338 AA; 145150 MW; F90CB3D104AF3955 CRC64;
MLEALLILVV LFAVWLMAAL LSFNPSDPSW SQTAWHEPIH NLGGAPGAWL ADTLFFIFGV
MAYTIPVIMV GGCWFAWRQR GNEDYIDYFA VALRLIGVLA LILTSCGLAA INADDIWYFA
SGGVIGSLLS TALQPMLNSS GGTIALLCVW AAGLTLFTGW SWVSIAEKIG SVVLTVLTFA
SNRTRRDDTW QDEDDYEDDE EHDEYEEDER EPQQAKGESR RARILRGALA RRQRLADKFS
NPVARKTDAA LFSGKRMDDA DEVQYSVRGT PADADDVLFS GHKVTEPDAF YDENDPLLNG
HSIADPAAVA AAATPVAPVW ASAQTAMPSE AVNVQAPDVA PEIEWHSAPS APQSHPGIAP
EPDYYAQPPV AQAPLQEEAY WQPAPNSAPV APAYQPAQQP QPYQAQQPHP GAYQPAPHDP
YAEPQAEHSA PAPDPYAPYA SYAAPEPYAP AQEAAPVYEP EPVAPPEEVK PARPPLYHFE
EVEAQRARER EQLAAWYQPI PEPEELTRKP EPIRAPEPAP AAPSFSAADI AGAAASGLNV
AAQGAAAAAS VHAASQATSA AAQTAAVAFT PVAGEAPRPQ VKEGIGPQLP RPNRVRVPTR
RELASYGIKL PSQRMAEERA REEAERRMAQ QQHGVSDEEA DAMYQDELAR QFAASQQQRY
GEEYQAEMSP EDEDAAEQAE LARQFAASQQ QRYSAAQPSG AAPFAPDETA YSPTTRVSES
PSQPLFMPEP AAPQPHHPVP PSQTQHYQQP PQQPPAHVAP AQSYAPPQGY TPQPQAPQGY
AQPTAAHQPQ PAAPTQGYQP PSAPAQYQAP SPAAPVQAQQ PASPRDSLIH PLLMRNGEEL
PKHKPSTPLP SLDLLTSPPA EVEPVDTFAL EQMARLVEAR LADFRIKADV VNYSPGPVIT
RFELNLAPGV KAARISNLSR DLARSLSTVA VRVVEVIPGK PYVGLELPNK KRQTVYLREV
LDCAKFRDNP SPLSVVLGKD IAGDPVVADL AKMPHLLVAG TTGSGKSVGV NAMILSMLYK
ATPEDVRFIM IDPKMLELSV YEGIPHLLTE VVTDMKDAAN ALRWSVNEME RRYKLMSALG
VRNLAGYNEK IAEAKRMGRP IPDPYWKPGD SMDATHPVLE KLPYIVVLVD EFADLMMTVG
KKVEELIARL AQKARAAGIH LVLATQRPSV DVITGLIKAN IPTRIAFTVS SKIDSRTILD
QGGAESLLGM GDMLYSGPNS SMPVRVHGAF VRDEEVHAVV QDWKARGRPQ YVDGITSDSE
SEGGGGGFDG GEELDPLFDQ AVSFVVEKRK ASISGVQRQF RIGYNRAARI IEQMEMQGIV
SEQGHNGNRE VLAPPPFE
//
