ID   C0QLS4_DESAH            Unreviewed;       753 AA.
AC   C0QLS4;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=FtsK2 {ECO:0000313|EMBL:ACN16378.1};
GN   Name=ftsK2 {ECO:0000313|EMBL:ACN16378.1};
GN   OrderedLocusNames=HRM2_33030 {ECO:0000313|EMBL:ACN16378.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN16378.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN16378.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; CP001087; ACN16378.1; -; Genomic_DNA.
DR   RefSeq; WP_015905140.1; NC_012108.1.
DR   AlphaFoldDB; C0QLS4; -.
DR   STRING; 177437.HRM2_33030; -.
DR   KEGG; dat:HRM2_33030; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_10_7; -.
DR   Proteomes; UP000000442; Chromosome.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT   DOMAIN          411..610
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          148..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          32..97
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        153..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         428..435
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   753 AA;  84094 MW;  254E76E06260829F CRC64;
     MKKFKYSIDE DLLIIKTECG EYKFKIDDEM GLANAQRIAD LMVNEMEKVE KKFLGGRETV
     SPYAALLMSK LNLSDRYVQL ENRYNALVKE HEQTKALYLD QRKSGETYKQ ILEKKKISLR
     DVISEDLKRI TESLSFSRKI EDMAETLPDP APAQEDFQQQ PSMEKQSEQS LTQAMDPEPA
     LVEIPVEQSE PGPLEKTKIE TTPATLEEPV LAPGSEPLEE PVTGPEPEPK PEPEPESLIE
     SAIVLSQEPS YQLRINTPGR NFKSAMASVT TSSDEFQLPC LDFLKTSDVE IEVDHEAIRR
     DAELLEQKLG YFGIKGEVME VSPGPVITTF EYKPAPGIKI SKIVNLADDL ALALSALSIR
     IVAPIPGKDV IGVEIPNAKM SIVPFIDIVG SDEFKNNDSK IPICLGKDIV GNPVVVGLEK
     MPHLLIAGAT GTGKSVGLNA MITSILYKSS PDEVKFIMID PKRIELSLFN DIPHLITPVI
     TDMKKANTAL QWVVREMEFR YEMLAKLQVR NIEQYNQKIK TADLSEYDDD DTFEVFSYIV
     IIIDELADLM MTASKDIEFS LTRIAQMARA AGIHLILATQ RPSVDVLTGI IKANFPTRIS
     FQVSSKTDSR TIIDANGAET LLGRGDMLFV PPGTARLSRV HGTYLSEEEL VTITNFLKAQ
     GKPRYVMDVV TEREEDSAMD TVNMGDDDYD EKYQAALEYV FTTRQASISS VQRALRVGYN
     RAARIIDLME KKGIVGQSDG VKPRQVLIDR LDL
//