ID   I4D804_DESAJ            Unreviewed;       909 AA.
AC   I4D804;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=DNA segregation ATPase, FtsK/SpoIIIE family {ECO:0000313|EMBL:AFM41928.1};
GN   OrderedLocusNames=Desaci_3019 {ECO:0000313|EMBL:AFM41928.1};
OS   Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM41928.1, ECO:0000313|Proteomes:UP000002892};
RN   [1] {ECO:0000313|EMBL:AFM41928.1, ECO:0000313|Proteomes:UP000002892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22704 / JCM 16185 / SJ4
RC   {ECO:0000313|Proteomes:UP000002892};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; CP003639; AFM41928.1; -; Genomic_DNA.
DR   RefSeq; WP_014827921.1; NC_018068.1.
DR   AlphaFoldDB; I4D804; -.
DR   STRING; 646529.Desaci_3019; -.
DR   KEGG; dai:Desaci_3019; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_12_6_9; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000002892; Chromosome.
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   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}; 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        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          573..764
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          201..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         590..597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   909 AA;  99892 MW;  412E22B236552E61 CRC64;
     MRTNRKNVNT IGIKIASILI GLFSLLGLLG GLGFSIGKQI FLKISVIFGT HFAWVVLFFC
     FFSAVALWIY SVQLQSFRSR AQTTAKSIHP KAVAKAQPAS QVEGKPSKSW LTSSKSKSKY
     IEEGIPLPSG KLVNLHGFNH YFSSPEWVEI KEMDLDQAME MEELGRDFPS YFGTGETFMP
     KKSPKLTLLK GLDAYFEEVD KEEKSEDLTT QSENNRPSLL ETIKEKTSQP RPIFKSQADQ
     AEFLAQFKID RSSSGENKHD IPLVSSENDS AENLEDVEVN LESKPDQKMN MDNVFDSAAK
     FTTVTEGKRG SELLSDRETI PEVFADDSLQ SLPDKGKDKT VDITDAEMNS KSKIQPMIEH
     KLEPILEPRA ELILEPMSES EPIAISPTST SISKSGPKSD LMCEPISDLI SESIVDRSLE
     TQVPITFEDE PEESVRSDFL WETPDLSLLA PVPPHIPIQD SETSKRLEKV LLDFGVKAKV
     VDVTRGPVIT RYELAPAPGV KISKIVNLAD DIALGLAARD VRIEAPIPGK AAVGIEVPNK
     QARSVPFREV LEAASFQQHP SKLKVALGKD IADQAIVADL IKMPHLLVAG ATGSGKSVCI
     TSIINSILFN STPAEVKFLL VDPKMVELSQ YNGIPHLLAP VVVDPKKAAS ALKWIVKEME
     NRYELFAAAG VRDVVRYNKL KSDNQSSLAL PYIVVIIDEL ADLMLVAPGE VEEAICRLAQ
     MARAAGIHLV IATQRPSVDV ITGVIKANIP SRISFAVSSQ IDSRTILDAT GAEKLLGKGD
     MLYSPLGINK AIRVQGCLVT DEEVQRIISH WKSLGKPEYL DPERLFADTP EKSDDGNGPD
     DALFFEAGNL CLKTGFASTS LLQRRLKIGY TRAARLIDML EDLGVVGGFE GSKPRQVLIS
     MDEFSERFG
//