ID I0Q0W2_STROR Unreviewed; 742 AA.
AC I0Q0W2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=HMPREF1115_0812 {ECO:0000313|EMBL:EIC74914.1};
OS Streptococcus oralis SK610.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1095741 {ECO:0000313|EMBL:EIC74914.1, ECO:0000313|Proteomes:UP000004548};
RN [1] {ECO:0000313|EMBL:EIC74914.1, ECO:0000313|Proteomes:UP000004548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK610 {ECO:0000313|EMBL:EIC74914.1,
RC ECO:0000313|Proteomes:UP000004548};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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:EIC74914.1}.
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; AJKQ01000026; EIC74914.1; -; Genomic_DNA.
DR RefSeq; WP_000908861.1; NZ_AJKQ01000026.1.
DR AlphaFoldDB; I0Q0W2; -.
DR PATRIC; fig|1095741.3.peg.1571; -.
DR Proteomes; UP000004548; 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 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 408..604
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 189..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..677
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 742 AA; 81810 MW; 60FBDDC09928B726 CRC64;
MLISLGIALL LIIAALKLGA AGITLYNLIR LVVGSLAYVA IGGLLIYLFL FKWIRKQEGL
LSGFLCIFAG LLLIFEAYLV WKFGLEQSVL KGTLSQVMTD LTGMRVTSFA GGGLLGVGLY
IPISFLFSNI GSYFIGVLLI LVGALLVSPW SIYDVAAFIG TQFRSFMEKQ EQRKQERFIK
REEEKARQEA EEAARIQREQ EEQDALPLPP VDPETGEILS EVPDYDFPPI PEEEWIEPEI
ILPKTDFDVP YVEEDFEDEE VQVDFSAKEA LEYKLPSLQL FAPDKPKDQS KEKKIVRENI
KILEETFASF GIKVTVERAE IGPSVTKYEV KPAVGVRVNR ISNLADDLAL ALAAKDVRIE
APIPGKSLVG IEVPNSEIAT VSFRELWEQS QTKPENLLEI PLGKAVNGTA RTFDLSKMPH
LLVAGSTGSG KSVAVNGIIA SILMKARPDQ VKFMMVDPKM VELSVYNDIP HLLIPVVTNP
RKASKALQKV VDEMENRYEL FAKVGVRNIA GYNAKVEEFN AQSEYKQIPL PLIVVIVDEL
ADLMMVASKE VEDAIIRLGQ KARAAGIHMI LATQRPSVDV ISGLIKANVP SRVAFAVSSG
TDSRTILDEN GAEKLLGRGD MLFKPIDENH PVRLQGSFIS DDDVERIVNF IKAQADADYD
DSFDPGDVPD NEGDFSDGEA GGDPLFEEAK ALVIETQKAS ASMIQRRLSV GFNRATRLME
ELEMAGVIGP AEGTKPRKVL QQ
//
