ID E1GUU5_9BACT Unreviewed; 820 AA.
AC E1GUU5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:EFN91557.1};
GN ORFNames=HMPREF9018_0587 {ECO:0000313|EMBL:EFN91557.1};
OS Prevotella amnii CRIS 21A-A.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=679191 {ECO:0000313|EMBL:EFN91557.1, ECO:0000313|Proteomes:UP000016016};
RN [1] {ECO:0000313|EMBL:EFN91557.1, ECO:0000313|Proteomes:UP000016016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIS 21A-A {ECO:0000313|EMBL:EFN91557.1,
RC ECO:0000313|Proteomes:UP000016016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (SEP-2010) 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:EFN91557.1}.
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DR EMBL; ADFQ01000031; EFN91557.1; -; Genomic_DNA.
DR RefSeq; WP_008448147.1; NZ_ADFQ01000031.1.
DR AlphaFoldDB; E1GUU5; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000016016; 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 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 462..668
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 720..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 820 AA; 90694 MW; D7AE76B25F19143F CRC64;
MVRKKTERTS KTFIEALGVK SIFNDKTGLI IGLLLVLLAI YICFAFFSYF STGQADQSLV
TDLRPGELKN TGQEFQNICG SLGAMISYFF ISRCFGIPAF FIPAFITLCG VKMIGAYKNV
NLWKWFLGMA LCMIWLSITF AKFLTPLMNN QIFNPGGDHG AYSVHFIENF VGTPGLIVLL
VIVLVAFLTY LTSETITVIR RIINPIGYLR DKVKFTVVNK DKGTISNTEE TLINDSPLSN
EEIYCNDSTD TNKKEYVELT IPNTAAQGNI SESIIKKPIN KKNARGDIGL EVKIAKAEEK
ANSPIVANST DIDTPINPRE PFTKWKYPTL NLLKEYDSDT HINYVGKDEL EANKNRIIKV
LNDFGVQIRS IRATVGPTIT LYEITPAQGI RISKIKNLED DIALSLAAIG IRIIAPMPGK
GTIGIEVPNA KPSIVSMFSI LNSKKFQESN MDLPIALGRT ITNDVFMVDL AKIPHLLVAG
ATGQGKSVGL NAIITSLLYK KHPNELKIVL VDPKKVEFSV YSPIAKSFMA AIDDNEDEPI
ITDVKKVVKT LKGLCVLMDE RYDMLKAAGA RNLKEYNHKF LNHHLNPEEG HKFMPYIVVI
IDEFGDLILT SGREIEMPIT RIAQLARAVG IHMIIATQRP TATIITGNIK ANFPGRIAFR
VGSMIDSRTI LDRPGAQQLV GRGDMLYLNG GEPVRVQCAF VDTIEVDKVN KFIANQPGPI
HPLEIPEPIS EDDNSNTEGL DTNNVDPLFE DAARTIVVTQ QGSTSMIQRR FSIGYNRAGR
LMDQLESAGI VGAAQGSKPR EVLISDENSL EALLTTLRHH
//
