ID F9P3T8_STRMT Unreviewed; 742 AA.
AC F9P3T8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=HMPREF9178_1893 {ECO:0000313|EMBL:EGR92356.1};
OS Streptococcus mitis bv. 2 str. F0392.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=768726 {ECO:0000313|EMBL:EGR92356.1, ECO:0000313|Proteomes:UP000003771};
RN [1] {ECO:0000313|EMBL:EGR92356.1, ECO:0000313|Proteomes:UP000003771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0392 {ECO:0000313|EMBL:EGR92356.1,
RC ECO:0000313|Proteomes:UP000003771};
RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (JUL-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:EGR92356.1}.
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DR EMBL; AFUO01000002; EGR92356.1; -; Genomic_DNA.
DR AlphaFoldDB; F9P3T8; -.
DR PATRIC; fig|768726.4.peg.1769; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000003771; 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..212
FT /note="Disordered"
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; 81578 MW; 9691B11D92F1016C CRC64;
MLISLGIALL LIIAALKLGA AGITLYNLIR LVVGSLAYVA IGALLIYLFL FKWIRKQEGL
LSGFLCIFAG LLLIFEAYLV WKFGLEQSVL KGTLAQVMTD LTGIRVTSFA GGGLLGVGLY
IPIAFLFSNI GSYFIGVLLI LVGALLVSPW SIYDVAAFIG AQFRSFMEKQ EQRKQERFIK
REEEKARQEA EEAARIQREQ EEQDALSLPP VDPETGEILS EVPVYDLPPI PEEEWIEPEI
ILPQADFEVP DVEEDFEDEE VQVDFSAKEA LEYKLPSLQL FAPDKPKDQS KEKKIVRENI
KVLEETFASF GIKVTVERAE IGPSVTKYEV KPAVGVRVNR ISNLADDLAL ALAAKDVRIE
APIPGKSLVG IEVPNSEIAT VSFRELWEQS QTKPENLLEI PLGKAVNGTA RTFDLSKMPH
LLVAGSTGSG KSVAVNGIIA SILMKARPDQ VKFMMVDPKM VELSVYNDIP HLLIPVVTNP
RKASKALQKV VDEMENRYEL FAKVGVRNIA GYNAKVEEFN SQSEYKQVPL PLIVVIVDEL
ADLMMVASKE VEDAIIRLGQ KARAAGIHMI LATQRPSVDV ISGLIKANVP SRVAFAVSSG
TDSRTILDEN GAEKLLGRGD MLFKPIDENH PVRLQGSFIS DDDVERIVNF IKAQADADYD
DSFDPGEVSE NDGDFADGEA GGDPLFEEAK ALVIETQKAS ASMIQRRLSV GFNRATRLME
ELELAGVIGP AEGTKPRKVL QQ
//
