ID A0A139TV68_9BACT Unreviewed; 841 AA.
AC A0A139TV68;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:KXU55552.1};
GN ORFNames=HMPREF3039_00283 {ECO:0000313|EMBL:KXU55552.1};
OS Akkermansia sp. KLE1798.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=1574265 {ECO:0000313|EMBL:KXU55552.1, ECO:0000313|Proteomes:UP000070454};
RN [1] {ECO:0000313|EMBL:KXU55552.1, ECO:0000313|Proteomes:UP000070454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1798 {ECO:0000313|EMBL:KXU55552.1,
RC ECO:0000313|Proteomes:UP000070454};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KXU55552.1}.
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; LTZM01000007; KXU55552.1; -; Genomic_DNA.
DR RefSeq; WP_067573543.1; NZ_KQ971067.1.
DR AlphaFoldDB; A0A139TV68; -.
DR PATRIC; fig|1574265.3.peg.263; -.
DR Proteomes; UP000070454; 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: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 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; 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; 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 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 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 465..701
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 228..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 482..489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 841 AA; 92669 MW; 2FF9B295E7E442F3 CRC64;
MALDAQERHV FEHEEDHPPV WMGMAWGAVS VLAGAALLAS MLTFDVREIG WNYLNKSGEV
MEGTTNLLNV VGLYGAGIVY WVLGGMAWML VILLAWWGCY RFTHRGRLTR GVIYGGVFLL
VSGCLFLTAG HVTGAEWVER HQVLGAGGLV GNLLGTHLLV PLAGVSAILA VSGLGYIIAL
IYAAGLRPRP LFRAVLREFR SWRMNRKEKK MERRSSQLAR EAARVRASME DAALSSPSPA
RRSRESSSRL HRTGDDLEGL YNEVAAAPSV RMPAPPKKSS APRTQGNLPL TTTPKITVAE
PAEIKPAPKV QPFAKIATPP TEEFKDYQLP GFELLHYEEK PDGPTDADRE EMLEIQQKII
ETLTTFRVDV TPGDITRGPT ITRYEVYPAR GVRVNTFDQY SKDIALATRA ESVNIVAPIP
GKDTVGIEIV NRKKVAVPLR ELLQDPEFCS PKKKIPLALG KDVYGRTVIG DLASMPHLLV
AGATGSGKSV CINSIISSML LKFRPDELRL ILVDPKVVEM QPYSKLPHLI VPVVTDPKKV
PNALRWCVNE MEHRYHCFAK VGVRNFEAFN KRPPEMPAEE EEEPESGEVD EELAESIARE
LESQGEWPAE EDDELDLDDD GVIPERFPYI VIIIDELADL MQTVGADIET NIGRLTQKAR
AAGIHLIVAT QTPRRQVVTG TIKANIPTRI AFQVASGTDS RVILDRQGAE KLVGKGDLLY
LPPGSAQVER AQGAFISDDE VEALVAHCAS QARQKFHEEV QKTLDEASHG GADSPLDDAE
EECYAKCLEV AVVERKVSTS LLQRRLSIGY GRAARMMDLL ESRGIIAPAD NTNRPRKVLV
E
//