ID A0A1S6QG50_9LACO Unreviewed; 773 AA.
AC A0A1S6QG50;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=PL11_000860 {ECO:0000313|EMBL:AQW20586.1};
OS Lentilactobacillus curieae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1138822 {ECO:0000313|EMBL:AQW20586.1, ECO:0000313|Proteomes:UP000030361};
RN [1] {ECO:0000313|EMBL:AQW20586.1, ECO:0000313|Proteomes:UP000030361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC M 2011381 {ECO:0000313|EMBL:AQW20586.1,
RC ECO:0000313|Proteomes:UP000030361};
RX PubMed=26021929;
RA Wang Y., Wang Y., Lang C., Wei D., Xu P., Xie J.;
RT "Genome Sequence of Lactobacillus curieae CCTCC M 2011381T, a Novel
RT Producer of Gamma-aminobutyric Acid.";
RL Genome Announc. 3:0-0(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}.
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DR EMBL; CP018906; AQW20586.1; -; Genomic_DNA.
DR RefSeq; WP_035168590.1; NZ_CP018906.1.
DR AlphaFoldDB; A0A1S6QG50; -.
DR KEGG; lcu:PL11_000860; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000030361; Chromosome.
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:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
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}; 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:UP000030361};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 439..635
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 218..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 456..463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 773 AA; 83967 MW; 27554085E5C6261E CRC64;
MAAKKKRRKT IKRKTSSKKS TGFFARYWVN ITGIIIILLA ISGLFSAGMV GAFVVNCVRF
FLGSLYVVGL IGVLAVGIAL AGFSKVPAIP VRIWSGTLLL LLGITLWLTL IQYTSAPQPV
NFVTANWEKL LDDVNSANVN SDIGGGIIAA ALFAGIKLLL GKIGVGIISS LLILVGLFVL
FNVSASKAFL AIKESVVFCG LSLKKFFNLG KSAGKTAKQK LASKQHQQST PVAQETSSMP
VGDDQHDDAP FSPADITVSG MAVADKKPVE DKQPEKKKKS KNTPEIDEPK HEVQLVDVQE
DDNYKLPTPD LLTKIDQNDQ SAELKSIDKN AKILQETLNS FGVKAQIKHV SLGPSVTKYE
LHPDIGVKVS RIVNLADDIA LALAAKDIRI EAPIPGKSLI GIEVPNRQIA TVSFRDVVEA
SPDNHGHLLQ VPLGKDVNGN VITADLTKMP HLLIAGSTGS GKSVAINGII TSILLNAKPS
QVKLMLIDPK KVELGVYNGI PHLLSPVVSE PKKAARALQK VVSEMENRYE LFAKYGQRKI
STYNEFVAKN NQQNDVKLQP MPYIVVIVDE LADLMMTVSN DVEAAIIRLA QMGRAAGIHM
ILATQRPSVD VITGLIKANV PSRIAFAVSS GIDSRTIIDT NGAEKLLGRG DMLFLPIDSN
TPVRVQGAFI PDKDVSTVVD FITDQASAEY DESMMVSDEE IKEEDQSDSD DDLFNDALEF
VVDQQKASTS LLQRHFRIGY NRAARLIDDL EQRGYIGPQD GSRPRQVFKQ KPE
//
