ID A0A0R2D818_9LACO Unreviewed; 795 AA.
AC A0A0R2D818;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=FC24_GL001860 {ECO:0000313|EMBL:KRM96694.1};
OS Loigolactobacillus rennini DSM 20253.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423796 {ECO:0000313|EMBL:KRM96694.1, ECO:0000313|Proteomes:UP000051638};
RN [1] {ECO:0000313|EMBL:KRM96694.1, ECO:0000313|Proteomes:UP000051638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20253 {ECO:0000313|EMBL:KRM96694.1,
RC ECO:0000313|Proteomes:UP000051638};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:KRM96694.1}.
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DR EMBL; AYYI01000053; KRM96694.1; -; Genomic_DNA.
DR RefSeq; WP_057874300.1; NZ_AYYI01000053.1.
DR AlphaFoldDB; A0A0R2D818; -.
DR STRING; 1423796.FC24_GL001860; -.
DR PATRIC; fig|1423796.3.peg.1889; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000051638; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; 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; 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; 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:0000313|EMBL:KRM96694.1};
KW Cell division {ECO:0000313|EMBL:KRM96694.1};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000051638};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 454..650
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 471..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 795 AA; 86462 MW; 547D5F43EA20C68D CRC64;
MATRRKPRRK RTSKAKKRRK TTAKKNSMYT VNIIGLIFVL LGLFATFKWG FVGNQLANLM
RIIAGDTFPA LAILLGVYGL FLLVVGRGPV LSGKRIGGTL LAYFSFLCFL DAVMFTQLEL
HSQFVPVTWR FLVADFQRAS VTTTIGGGML GALGYSASYF LVGQFGTYLL TVVGILTGLF
LLFDIPFVVV KAAVTQIVRV VHWFGRQLMS LLKRLGMAGQ KISPQLKRLK KTSKKPKSLR
PAPTKQPAES TVAATAEKSD QSSTQSAAPA PTINVASKQM NAPQSQQAKV DLDQLAAPTS
AAPESATPAL VQVEADEDYQ LPQADLLQAI PPTDQSAEYA TIKQNTKKLK QTFDSFGIDV
EVKNVNLGPA VTKYEIKPAI GVKVSKIVSL TDDLALALAA KDVRIEAPIP GKSLIGIEVP
NKAVATVSYR DVYQSQPAHP GKLLTVPIGR DISGKVIMID ITKMPHLLIA GSTGSGKSVM
INDIITGLLM TAKPHEVKMM MIDPKKVELS VYNGVPHLLT PVVSNAKKAA QALHKAVAEM
ERRYELFAQS GKRNITEYNQ AVQQQDAATE QPLPAMPYIV VIVDELADLM MVSSNEVEDA
IVRLAQMGRA AGIHMILATQ RPSVDVITGL IKANIPSRMA FAVSSGVDSR TIIDSTGAEK
LLGRGDMLYL PMGQNKPTRV QGAYISAKDV EAVVKFITAQ QTADYDERLT PDDKPEAEKA
LEAEDELFPD AVKLVAQLQT ASISMLQRRF RIGYNRAARI VDEMEQRGIV GPAAGSKPRQ
VFVQKPDDEQ PQQKS
//
