ID A0A1W1YDL2_9FIRM Unreviewed; 979 AA.
AC A0A1W1YDL2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=4TM region of DNA translocase FtsK/SpoIIIE {ECO:0000313|EMBL:SMC34242.1};
GN ORFNames=SAMN06296952_0443 {ECO:0000313|EMBL:SMC34242.1};
OS Oscillospiraceae bacterium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=2485925 {ECO:0000313|EMBL:SMC34242.1, ECO:0000313|Proteomes:UP000192633};
RN [1] {ECO:0000313|Proteomes:UP000192633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHP2 {ECO:0000313|Proteomes:UP000192633};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
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; FWXP01000001; SMC34242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1YDL2; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000192633; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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 GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; 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; 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; 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}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 631..821
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT COILED 509..536
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 648..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 979 AA; 107486 MW; F34BBD814B4F74A8 CRC64;
MSSNREDTKE LVGLALFFCA VVITLLYYLP ENITGFLGEW IRGLGFGLIG SAAFMIPLFF
LYAAIDFFLE KREGVAPIRI RSVIISMICV ASLFALFSMD FDYFKTLCVV EGAEDKFRAT
KALALLWKSG PDASLIVKDP EMKHCLPGGL VGGGIAVAMN KLAGKTISIL AMFVMLLSQI
ILMFHVSLKQ TVKKTAHAIG RTATKAYNNM RTPSRPQQRP PYGNQRQMMP AQNVYRRHSS
VPNNAKSPFV NTPTETYGVP LFDVDYQNNN RNQNYRDPFA KRIPVDSKTG FMDVSAKEFG
ADTSVDNSRL NYENRQVSTE GSMDAPKAEF DYNALPKNRP LTPRHKEVEE PEFLRHPDAQ
QDFYDLNNGV YADQQQGTYD ENSYQNEYYE DVQDDLPFEI TDDDPYDYSP ERSVRKPHIS
MKPQVQVDTY EPQETYNESP AVNEAPSISI NSAVDDQETG FNTEGRIIKT AEAPAPTVEI
TSGRVPAYKG RRKGPYKPAP INLLAKEEKQ VNANNNAELQ EKAHELEDAL QSFGINAKVV
NITHGPAITR FELTIDRGVK VSRVLSLQDD IALAMAAVSV RIEAPIPGKS AIGIEIPNKK
TSAVQLRGLL ETREFKAGPG LEVPLGKDIP GRPIMCNIAK MPHLLIAGST GSGKSVCINT
ILTSILCKAS PDDVRMILID PKVVELSIYN DIPHLLMPVV TDPKKAANAL SWAVIEMERR
YKCFAESKVR DLSGYNNFLK AQGEQPLPLI LIVIDELADL MTVAAKDVED KISRLAAMAR
AAGLHLLIAT QRPSVDVITG VIKANVPSRI AFAVSSGVDS RTILDSVGAE KLLGKGDMLY
APLSAPKPVR GQGAFVSDGE VESIVKFLKD NYGQMYDEAI MNAVNSQNVG AAQSTGGGDA
GSGSDEDDLL DQAVNIVIEA GNASVSILQR RLGVGYPRAA RLIDVLEQKH IIGPFEGSKP
RKVLVTKTDW LEMQSKGDS
//
