ID F5VVS7_STROR Unreviewed; 786 AA.
AC F5VVS7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN Name=spoIIIE {ECO:0000313|EMBL:EGL88054.1};
GN ORFNames=HMPREF9968_0833 {ECO:0000313|EMBL:EGL88054.1};
OS Streptococcus oralis SK255.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1005704 {ECO:0000313|EMBL:EGL88054.1, ECO:0000313|Proteomes:UP000003695};
RN [1] {ECO:0000313|EMBL:EGL88054.1, ECO:0000313|Proteomes:UP000003695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK255 {ECO:0000313|EMBL:EGL88054.1,
RC ECO:0000313|Proteomes:UP000003695};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:EGL88054.1}.
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DR EMBL; AFNM01000036; EGL88054.1; -; Genomic_DNA.
DR AlphaFoldDB; F5VVS7; -.
DR PATRIC; fig|1005704.3.peg.1321; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000003695; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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; 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}; Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW 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 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 452..648
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 234..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..721
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 786 AA; 86894 MW; CFCD2BBDBA9C3646 CRC64;
MQSFLISLDV SEIWYNRSMA NKNTSKTRRR PSKAELERKQ AIQRMLISLG IALLLIIAAL
KLGAAGITLY NLIRLLVGSL AYVAIGGLLI YLFLFKWIRK QEGLLSGFLC IFAGLLLIFE
AYLVWKFGLE QSVLKGTLAQ VMTDLTGMRV TSFAGGGLLG VGLYIPISFL FSNIGSYFIG
VLLILVGALL VSPWSIYDVA AFIGAQFRSF MEKQEQRKQE RFIKREEEKA RQEAEEAARI
KREQEEQDAL PLPPVDPETG EILSEVPDYD LPPIPEKEWS EPEIILPQAD FDVPDVEEDF
EDEEVQVDFS AKEALEYKLP SLQLFAPDKP KDQSKEKKIV RENIKILEET FASFGIKVTV
ERAEIGPSVT KYEVKPAVGV RVNRISNLAD DLALALAAKD VRIEAPIPGK SLVGIEVPNS
EIATVSFREL WEQSQTKPEN LLEIPLGKAV NGTARTFDLS KMPHLLVAGS TGSGKSVAVN
GIIASILMKA RPDQVKFMMV DPKMVELSVY NDIPHLLIPV VTNPRKASKA LQKVVDEMEN
RYELFAKVGV RNIAGYNAKV EEFNAQSEYK QVPLPLIVVI VDELADLMMV ASKEVEDAII
RLGQKARAAG IHMILATQRP SVDVISGLIK ANVPSRVAFA VSSGTDSRTI LDENGAEKLL
GRGDMLFKPI DENHPARLQG SFISDDDVER IVNFIKAQAD ADYDESFDPG EVSENEGEFS
DGEAGGDPLF EEAKALVIET QKASASMIQR RLSVGFNRAT RLMEELEMAG VIGPAEGTKP
RKVLQQ
//
