ID A0A0N1B2H7_9SPHN Unreviewed; 807 AA.
AC A0A0N1B2H7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=IP79_09025 {ECO:0000313|EMBL:KPF63933.1};
OS Porphyrobacter sp. AAP60.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=1523423 {ECO:0000313|EMBL:KPF63933.1, ECO:0000313|Proteomes:UP000037996};
RN [1] {ECO:0000313|EMBL:KPF63933.1, ECO:0000313|Proteomes:UP000037996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP60 {ECO:0000313|EMBL:KPF63933.1,
RC ECO:0000313|Proteomes:UP000037996};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPF63933.1}.
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DR EMBL; LJHV01000008; KPF63933.1; -; Genomic_DNA.
DR RefSeq; WP_054118869.1; NZ_LJHV01000008.1.
DR AlphaFoldDB; A0A0N1B2H7; -.
DR STRING; 1523423.IP79_09025; -.
DR PATRIC; fig|1523423.3.peg.2913; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000037996; 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:KPF63933.1};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 441..660
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 458..465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 807 AA; 86818 MW; 30CA0E4C8963A040 CRC64;
MASRAAQTVK PGRQTSARRS DAEWRAGLRR TLRRLAQMTG AGVLFGAAVF LALALASYTQ
TDPSPSTAAD PAQVANWMGT SGAWAADRVL LIFGLPGVLL LPLLYISARK LWRDVENGDT
PETTPWWLPT ALLLLAMTLI ATVLALAFAG PGGTLPAQAG GLAGLLGAGA IEAVAARFGD
EAQGWIILGA ALLSLAVGVG LLTRIFAIDW RVLLSLPEFL GGGSLSGLMR RLPLPGRSAA
PALTFAGDED AEDAPAARPR RAVKGGEPVP FEPAPRRAPE ISDPSAPPKR AAPAKTAQGD
MFAAFNLPSL DLLAEPPVDK GPKLDKLALE RNARLLENVL DDFNVKGEIT AVRTGPVVTM
YELEPAPGIK ASRVVGLAED IARNMSAISA RVSPIPGRTV MGIELPNQDR QVVMLKELAA
CADFADAKGS LPIILGKDIA GEPIIADLAA MPHLLVAGTT GSGKSVGLNV ILLSLLYRFT
PTELRLILID PKVLELKTYD DIPHLLSPVV TEPHKSVRAL KWAVEEMERR YRMMSAISSR
NIHSFNEKVS AAIAKGKPLG RRVQTGFDPE TGEQLFEEEQ LDYQPLPQIV LIVDELADLM
VTIGKEIEVL IQRLSQKSRA AGIHLIMATQ RPSVDVITGV IKANLPTRIS FKVTSRIDSR
TILGEQGAEQ LLGKGDMLYK PNTGAMVRVH GPFVSDEEVE AVADFWRSQG APEYVDAVTE
EPEDGGGFGF EDDMTASDNP EERKYRQACQ VVIENQKASG SWLQRQMGVG YNTAAKWIER
MEEDGLVGPA NHVGRREIYR DRDGNPL
//
