FTSK_BRUME
ID FTSK_BRUME Reviewed; 817 AA.
AC Q8YJB8;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=BMEI0168;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Located at the septum.
CC {ECO:0000250}.
CC -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for the
CC localization to the septal ring and is required for cell division,
CC followed by a linker domain, and a C-terminal domain, which forms the
CC translocation motor involved in chromosome segregation. The C-terminal
CC domain can be further subdivided into alpha, beta and gamma subdomains.
CC The alpha and beta subdomains multimerise to produce a hexameric ring,
CC contain the nucleotide binding motif and form the DNA pump. The gamma
CC subdomain is a regulatory subdomain that controls translocation of DNA
CC by recognition of KOPS motifs and interacts with XerD recombinase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL51350.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL51350.1; ALT_INIT; Genomic_DNA.
DR PIR; AC3273; AC3273.
DR RefSeq; WP_005970682.1; NZ_CP007763.1.
DR AlphaFoldDB; Q8YJB8; -.
DR SMR; Q8YJB8; -.
DR STRING; 224914.BMEI0168; -.
DR EnsemblBacteria; AAL51350; AAL51350; BMEI0168.
DR GeneID; 29593885; -.
DR KEGG; bme:BMEI0168; -.
DR KEGG; bmel:DK63_1268; -.
DR PATRIC; fig|224914.52.peg.1336; -.
DR eggNOG; COG1674; Bacteria.
DR OMA; IGPANHA; -.
DR Proteomes; UP000000419; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..817
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098243"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 452..671
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 252..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 817 AA; 88806 MW; 7F94030AACA316DF CRC64;
MRQGYSPSYP LRDERITEDR LRFANLVRRQ VYILLGLGLL SLTAMAVGAL ATWNVADPSF
SHATDNPVTN ALGYPGAVFS DLAMQFFGLA SVPALLPLAV WSLLLMIRGY IGRIARRSLA
WVGAALLFAA IASCFAVPQS WPMPIGLGGV FGDMLLRIPG FFLGGFPQGA IASAIALVLA
FPALWFCFFA SGIIGRGAEA VNPAMLSANR SADDEFADED ADNEAGGGFH FIGALTHLVL
MTTATIRRMT GLGRRRSRED DFDDMRMVRR SAETRNAPPP RARKARVEQT APSPKPGPRA
QREAQPSFLK DNGIFEMPSL HFLAEPKLVQ RDPALSKDAL EQNARLLAGV LEDFGVRGEI
INVKPGPVVT LYELEPAPGI KSSRVIGLAD DIARSMSAIA ARVAVIPGRN AIGIELPNPK
REMVYLREML ASRDFEQSKA KLALALGKTI NGEPVIADIA KMPHVLVAGT TGSGKSVAIN
TMILSLLYRM TPQECRLIMI DPKMLELSVY DGIPHLLTPV VTDPKKAVVA LKWTVREMED
RYRKMSKVGV RNIDGFNQRV GLAQKKGEPI ARTVQTGFDR NTGEAIYETE ELDLEPMPYI
VVIIDEMADL MMVAGKDIEG AVQRLAQMAR AAGIHVIMAT QRPSVDVITG TIKANFPTRI
SFQVTSKIDS RTILGEQGAE QLLGQGDMLF MAGGGRIQRV HGPFVGDDEV ERIVQHLKLQ
GVPEYLDAIT EDEDDDEGGS GPAGTGNLED SDDPYDQAVA VVLRDKKAST SYIQRRLGIG
YNRAASIIER MEDEGIVGPA NHAGKREILV PTGDDDF
