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Database: UniProt
Entry: A0A3D8N098_9DELT
LinkDB: A0A3D8N098_9DELT
Original site: A0A3D8N098_9DELT 
ID   A0A3D8N098_9DELT        Unreviewed;       929 AA.
AC   A0A3D8N098;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:RDV39577.1};
GN   ORFNames=DV096_03130 {ECO:0000313|EMBL:RDV39577.1};
OS   Bradymonadaceae bacterium TMQ3.
OC   Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae.
OX   NCBI_TaxID=2283320 {ECO:0000313|EMBL:RDV39577.1, ECO:0000313|Proteomes:UP000256871};
RN   [1] {ECO:0000313|EMBL:RDV39577.1, ECO:0000313|Proteomes:UP000256871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMQ3 {ECO:0000313|EMBL:RDV39577.1,
RC   ECO:0000313|Proteomes:UP000256871};
RA   Wang S.;
RT   "Lujinxingia celare sp. nov., isolated from a marine island.";
RL   Submitted (AUG-2018) 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}.
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:RDV39577.1}.
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DR   EMBL; QRGZ01000001; RDV39577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8N098; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000256871; 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   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        91..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          570..789
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         587..594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   929 AA;  100705 MW;  4FDBB9A416454053 CRC64;
     MAAKSAASSS SKKKSTARSS SSKTTSSKAK AAPRVNGTSF ALQRELSGVV LLALALVLLL
     SIASFNPADL IRGEAPPTNL IGPVGVWVGD VLLTIFGLGA FFLNALLWYF GISMLLGREI
     EARPGEIIGQ LLFVLSGTVL GHLALSGYLV LGHEPGGWIG AFGGELMRGA VGTVGTAILA
     GSAFLIGAVL VTDLSPGAVA RWFAAHIHRF TAWMRHRRAV RREFKQRYQE ERDRLLAGEE
     LTIAEEARLE AERAVLGKTT RGYDFEESLD DEVERKVAGR LARLFGPRLR KAELATDDAP
     VSSVDASVDT PAKNAPEKKS KKSDDTKKAP SNPIPDDEGW EIGELATDAD IKAEPIPIAG
     LDEAGPSEEA IEVSDTQVID MRSEREASAP VKGDFGPQIV ESEATRKARE RQQMLESDAE
     GGLLFKPQKK GNYELPPISF LNFDRGEEVA VDSDALRDMA AQIEKTLADF KVEGTVVEIC
     PGPVITMFEF SPAPGVKLSK IANLSDDLAM ALAAHSVRIV APIPGKGVVG IEVPNPSREM
     VYLKEIIADE AFADNKKMQL PLALGKDTEG GPVIADLAKM PHLLVAGATG AGKSVAVNTM
     VCSLLYKHTP DDVRMIMVDP KMLEFSIYAD IPHLLLPVVT DPKQATVALN WTVQEMERRY
     QALADMGVRN VTGYNDKIKK LTKQAELDQL NGLEDSEALR SLGIDHKGDP EHKHLPFIIV
     IIDEFADLMM TASKDVETAV ARLAQKARAA GIHLILATQR PSTDVITGLI KANFPTRLAL
     RVTSKTDSRV ILDANGAENL LGNGDMLFVP PGTSFLQRTH GAYVSEKEID KMVEFLKVQG
     EPNYDESILA DDGEDDESAV ADEDKDEFYE EAVRLVVESK QASISMLQRK LRVGYNRAAR
     MVDIMEIEGI VGESDGYKPR EVLVDQSPY
//
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