ID A0A0S8BMU7_9PROT Unreviewed; 768 AA.
AC A0A0S8BMU7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KPK12486.1};
GN ORFNames=AMJ68_01770 {ECO:0000313|EMBL:KPK12486.1};
OS Acidithiobacillales bacterium SG8_45.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703383 {ECO:0000313|EMBL:KPK12486.1, ECO:0000313|Proteomes:UP000053136};
RN [1] {ECO:0000313|EMBL:KPK12486.1, ECO:0000313|Proteomes:UP000053136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_45 {ECO:0000313|EMBL:KPK12486.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK12486.1}.
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DR EMBL; LJTU01000005; KPK12486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BMU7; -.
DR PATRIC; fig|1703383.3.peg.1469; -.
DR Proteomes; UP000053136; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; 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}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:KPK12486.1};
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 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 408..617
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 425..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 768 AA; 83810 MW; 6BD7ED0752823AC7 CRC64;
MSQATRKKNQ EPLLTPAVWR LLREAGFYVL TAIAIYLLLS LATYSPGDPS WSHSGPTGKI
HNLGGQAGAF VVDVLFNLFG FLAYLFPIMV GYGAWKVFQH RKDPDPPNLH HKIVIGTGFV
LLLVGACGLA TLHFDPLSRD LPFSSGGLLG DAVGSGLMAA FSHVGATIFL LALFLAGVTL
FTGISWFHVM DITGKAVWDV YSLVRSQISE RIDRAVGEQA KKEREEKVVQ VAKRLEKRAK
PKIEPVIHKV ETSARVERER QVPLFEVPTG AELPPLSLLD KPDEKKVQSF SEQSLENMAR
LLEKKLMDFN IEAVVVAVHP GPVITRFEID PAPGVKAAQI SNLASDLARS LSLVSLRVVE
NIPGKSYMGI EIPNESRETV RLSEILSSEA YETSHSPLGL ALGKDISGIP VVTDLAKMPH
LLIAGTTGSG KSVCINALIL SLVYKATPDQ VRLIMVDPKM LELATYEGIP HLLAPVVTDM
KQAANALRWC IFEMERRYRL MAALGVRNIG GYNRKVKDAE AKGKPIMNPF ALEGDEPEPL
KQLPFIVILI DELADMMMVV GKKVEEVIAR LAQKARAAGL HLIVATQRPS VDVITGLIKA
NIPARIAFQM SAKVDSRTVL DQMGAEQLLG QGDMLFLQPG MGVPQRIHGA FVSDEEVHRV
VAALKQIGEP IYNDDVLEGD PAQKADDSTF GAGLGIEGGD AEQDPLYDEA LRIVTETRRA
SISGVQRRLR IGYNRAARLI EEMERAGVVG ELQSNGQREV LAPPPPQD
//
