ID A0A0S7YB62_9BACT Unreviewed; 687 AA.
AC A0A0S7YB62;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=AMJ50_00390 {ECO:0000313|EMBL:KPJ71834.1};
OS Parcubacteria bacterium DG_74_3.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703767 {ECO:0000313|EMBL:KPJ71834.1, ECO:0000313|Proteomes:UP000051833};
RN [1] {ECO:0000313|EMBL:KPJ71834.1, ECO:0000313|Proteomes:UP000051833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_74_3 {ECO:0000313|EMBL:KPJ71834.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ71834.1}.
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; LJNG01000002; KPJ71834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YB62; -.
DR STRING; 1703767.AMJ50_00390; -.
DR PATRIC; fig|1703767.3.peg.54; -.
DR Proteomes; UP000051833; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IPR003593; AAA+_ATPase.
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; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SMART; SM00382; AAA; 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..531
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 668..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 358..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 687 AA; 75715 MW; 7E787C380CB29815 CRC64;
MLPQRVKKLI GGVMTFLIAI IVILSFFGKA GMVGEKFMKL SLLLIGSTIY ALPLFLALAG
AVFLNTQQRK FLGPVIFAIL ILTLGISGIF SLLNQDPQKG GFLGYIFSLP LLGLFGLLVT
KIIFFTLVIV GILIFWQLLV PSPSLDREKE EKTSVLTRVF GRAKRVPKFE VKEVPPLPSE
KVPEFKPKAP PLELKINKVS YKPSTSKYKL PPLDLLAQEK ETPSAGNTRT NAVIIKKTLE
NFGIPVEMAE INIGPTVTQY ALKPAEGIKL SKITALSNNL ALALASHPIR IEAPIPGRSL
VGIEVPNKIR ARVRLESLLS EPELQNSSSN LIFALGRGVS GKPDYADLAK MPHLLVAGAT
GTGKTIFLNN LILSFLYQNS PEFLRLILVD PKRVEFTAYG KLPHLLSPVI YDATKTVHCL
NWLISEMGRR FNVLAMEKVR DIAGYNEKVL KEGGEFMSYI VLIIDELADL IVAKGREIET
GIVRLAQLAR AVGIHLVVAT QRPSVEVITG LIKANITSRV SFQVASQIDS RTVLDMAGAE
KLLGLGDLLF LSAQTVKPKR IQGPYVSDKE VKKVTNWIVE NNQDMVLENG LYQDLRDSLE
KSEVEGLGLD QLSSFELAED PLYPETKKLV IETRRASASF LQRKLKIGYA RAARLLDILE
KRGIVGPPQG AKPREVYGGE DEPQEFI
//