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Database: UniProt
Entry: T0HSQ2_9SPHN
LinkDB: T0HSQ2_9SPHN
Original site: T0HSQ2_9SPHN 
ID   T0HSQ2_9SPHN            Unreviewed;       799 AA.
AC   T0HSQ2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=L284_02045 {ECO:0000313|EMBL:EQB19361.1};
OS   Novosphingobium lindaniclasticum LE124.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB19361.1, ECO:0000313|Proteomes:UP000015527};
RN   [1] {ECO:0000313|EMBL:EQB19361.1, ECO:0000313|Proteomes:UP000015527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LE124 {ECO:0000313|EMBL:EQB19361.1,
RC   ECO:0000313|Proteomes:UP000015527};
RX   PubMed=24029761;
RA   Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT   "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT   a Hexachlorocyclohexane Dumpsite.";
RL   Genome Announc. 1:e00715-13(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:EQB19361.1}.
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DR   EMBL; ATHL01000018; EQB19361.1; -; Genomic_DNA.
DR   RefSeq; WP_021232386.1; NZ_ATHL01000018.1.
DR   AlphaFoldDB; T0HSQ2; -.
DR   PATRIC; fig|1096930.3.peg.397; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000015527; 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: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:EQB19361.1};
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:UP000015527};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          433..652
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          229..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         450..457
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   799 AA;  86852 MW;  5FDF6B960D1A4516 CRC64;
     MATRPIAPGR RIAKPNWRAV LKRSLRRASE LSGALALFAA MTFLALSLVS YHQTDPSAST
     AAGGPAQNWM GSVGAWVAER ALVLFGPVAA LFVPLLYVFA RKLWLLVEED DNEIEHSNQR
     WWRPVAVLAI AMTLIATVMS MVFTAPGGVL PASMGGITGL LGAKGITGLA AFAPEVVQGW
     IKLVLALLCA LAGVALIGQV FAVDWLRLLT LPGRIGRLNK DGAPAPAKIA AAAAERAKPE
     EEADAKPRAA PRIDAPAMAD SAAERPRKAP EISDPKASPT PAQLNIGNRQ KDMFDKFALP
     GLDLLKDPPP NSQPKIDKLS LERNARLLET VLDDFNVKGE ITAVRTGPVV TMYELEPAPG
     IKSSRVIGLA DDIARNMSAI SARVSSIPGR TVMGIELPNA DRQMVSFKEM VASEAFANHK
     GMLPIILGKD IAGEPVVADL ATMPHLLVAG TTGSGKSVGL NTILLSLLYR LTPAQCRLIL
     VDPKVLELKS YDDIPHLLSP VVTEPPKAVR ALKWAVEEME RRYRQMSEIS VRNLASFNEK
     VRAAAAKGKP LGRRIQIGFD PETGEELYED RQLDYETLPQ IVLIVDELAD LMVTVGKEIE
     VLIQRLSQKS RAAGIHLIMA TQRPSVDVIT GVIKANLPTR VSFAVTSRID SRTILGEQGA
     EQLLGKGDML YKPSSDPVKR VHGPFVSDEE VEQVADHWRG QGKPDYVDAV TNEPEEGSFG
     FDDLDATASD QPEERKYRQV CQLVFENQKV SVSWLQRQMG VGYNTAAKWV ERMENDGYVG
     PANHVGRRDI YRDENGSPL
//
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