ID A0A1I3Y885_HALDA Unreviewed; 765 AA.
AC A0A1I3Y885;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:SFK28074.1};
GN ORFNames=SAMN04487936_11096 {ECO:0000313|EMBL:SFK28074.1};
OS Halobacillus dabanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=240302 {ECO:0000313|EMBL:SFK28074.1, ECO:0000313|Proteomes:UP000183557};
RN [1] {ECO:0000313|EMBL:SFK28074.1, ECO:0000313|Proteomes:UP000183557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3704 {ECO:0000313|EMBL:SFK28074.1,
RC ECO:0000313|Proteomes:UP000183557};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; FOSB01000010; SFK28074.1; -; Genomic_DNA.
DR RefSeq; WP_075037596.1; NZ_FOSB01000010.1.
DR AlphaFoldDB; A0A1I3Y885; -.
DR STRING; 240302.BN982_01990; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000183557; Unassembled WGS sequence.
DR GO; GO:0016020; C: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: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 Coiled coil {ECO:0000256|SAM:Coils};
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 55..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 429..625
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 258..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..224
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 263..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 446..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 765 AA; 84796 MW; 4300752F4667011E CRC64;
MAGKRKKKKK KSNIKSHMKF ELLGLFFLFI AVIGSGASAI SDGAIPGGLE RFWQFIFGVW
YFIASLFFLI VGVYLMVKRK WPTFLHKRLL GVYLIITALL LFTHLETLSA DLGTGEGSIF
AMTWDRITGM MRGELSFYSI GGGLSGAILL SITYYLFAKA GAAILSFFLL VVGIIFVSEK
SIGELFAKIG HKLKAISKDQ VERIKERRKE KAEEKQALPN EEEEAVVYEI NDTTGQQEEE
VTEQEPIIQD FTDNAYTKEG TGGAVDKSHE NQQEPDEVNL EKSMPTAELE NFDYHLPGLE
LLDEPTSTPQ SQGRSHIQAT VRKLEKTFQS FGVKAKVTKV HVGPSVTKYE VYPDVGVKVS
KIVNLNDDLA LALAAKDIRI EAPIPGKSAV GIEVPNQEVS MVSLREVLET GKSNPEAKLS
FALGRDISGE AVMSELNKMP HLLVAGATGS GKSVCINGII TSILMRAKPH EVKMMMIDPK
KVELNVYNGI PHLLAPVVTD PKKASRALKK VVSEMERRYD LFSDTGTRNI ESYNEYIKKY
NKENEEEQPQ LPYIVVLVDE LADLMMVASN EVEDAITRLA QMARAAGIHL IIATQRPSVD
VITGVIKANI PSRIAFSVSS QTDSRTILDS GGAEKLLGRG DMLFTPVGSN KPTRVQGAFL
SDEEVERIVD FCVEQQKAQY QEEMIPEEES EVKQEVDDDL YPEAVQMVIE MQSASVSMLQ
RRFRVGYTRA ARLIDAMEDN GIVGPYEGSK PRSVLVSQTE EQTTS
//
