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Database: UniProt
Entry: T0GHC5_9SPHN
LinkDB: T0GHC5_9SPHN
Original site: T0GHC5_9SPHN 
ID   T0GHC5_9SPHN            Unreviewed;       772 AA.
AC   T0GHC5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=L485_14280 {ECO:0000313|EMBL:EQB00087.1};
OS   Sphingobium baderi LL03.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB00087.1, ECO:0000313|Proteomes:UP000015524};
RN   [1] {ECO:0000313|EMBL:EQB00087.1, ECO:0000313|Proteomes:UP000015524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL03 {ECO:0000313|EMBL:EQB00087.1,
RC   ECO:0000313|Proteomes:UP000015524};
RX   PubMed=24051322;
RA   Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT   Sphingobium baderi Strain LL03T.";
RL   Genome Announc. 1:e00751-13(2013).
CC   -!- FUNCTION: Essential cell division protein that coordinates cell
CC       division and chromosome segregation. The N-terminus is involved in
CC       assembly of the cell-division machinery. The C-terminus functions as a
CC       DNA motor that moves dsDNA in an ATP-dependent manner towards the dif
CC       recombination site, which is located within the replication terminus
CC       region. Translocation stops specifically at Xer-dif sites, where FtsK
CC       interacts with the Xer recombinase, allowing activation of chromosome
CC       unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC       the direction of DNA translocation. FtsK can remove proteins from DNA
CC       as it translocates, but translocation stops specifically at XerCD-dif
CC       site, thereby preventing removal of XerC and XerD from dif.
CC       {ECO:0000256|ARBA:ARBA00024784}.
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:EQB00087.1}.
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DR   EMBL; ATIB01000071; EQB00087.1; -; Genomic_DNA.
DR   RefSeq; WP_021245488.1; NZ_KQ130471.1.
DR   AlphaFoldDB; T0GHC5; -.
DR   PATRIC; fig|1114964.3.peg.2798; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000015524; 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   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; 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, ECO:0000313|EMBL:EQB00087.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000015524};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          407..626
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          214..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         424..431
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   772 AA;  84123 MW;  DADD4B04D2514F5F CRC64;
     MAVSRGIKRT PEWREMLKRS LIRSGALIGS IALLLATLFL ALALLSYTPS DPSMNTVAGD
     QVRNVMQLPG AWTADFLLWL LGVPAALVLP LMAITARRLW GDQDMSEWKG QFGKCLTGIV
     LVGLALALFQ PDPLVGLPAG WGGVIALVFA RGIMSLSAQL PAFQGWAIGA LVVLTLVAGL
     YVWYRSLALE KPILALRRPA LPRLNLPRPA FALPGRVPAD EDEDEDGAER VIAPRKTVTN
     EPKPPITIQS PKPAPSQRPV APVSQDDLFG NSSLPSPDLL NPIPAGQGQK IDKAALERNA
     RLLESVLDDF HVKGNIVEVR PGPVVTMYEL EPAPGIKASR VIALADDIAR NMSALSARVA
     TIPGRTVIGI ELPNANREGV SFRELITSEQ FGQEATLPII LGKNISGEPI IADLAPMPHL
     LIAGTTGSGK SVGLNAMILS LLYRMTPDQL RLIMIDPKML ELSTYDDIPH LLSPVVTEPS
     KAIRALKWAV EQMEDRYRMM ASISVRNLAN YNEKVRAAKA KGKPLGRRVQ TGYDPETGKP
     IYEEEQLDFQ PLPQIVVVVD ELADLMMTAG KEVEFLIQRL AQKARAAGIH LILATQRPSV
     DVITGVIKAN LPTRISFFVT SKIDSRTILG EQGAEQLLGK GDMLYMHGGK GLMRVHGPFV
     SDDEVRVVAD HWRAQGQPDY ISAVTEEPEE GSFALDGVDL GDDSPDAQLY RKACQLVFEN
     QKASTSWLQR QLRVGYNSAA RLIERMEEDG LVGAPNHVGR REVLRDENGN PL
//
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