ID   A0A2R3JTH7_9LACO        Unreviewed;       843 AA.
AC   A0A2R3JTH7;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=C5Z26_01415 {ECO:0000313|EMBL:AVK62856.1};
OS   Lactobacillus sp. CBA3606.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=2099789 {ECO:0000313|EMBL:AVK62856.1, ECO:0000313|Proteomes:UP000238064};
RN   [1] {ECO:0000313|EMBL:AVK62856.1, ECO:0000313|Proteomes:UP000238064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBA3606 {ECO:0000313|EMBL:AVK62856.1,
RC   ECO:0000313|Proteomes:UP000238064};
RA   Jung M.Y.;
RT   "Complete genome sequence of Lactobacillus sp. CBA3606.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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; CP027194; AVK62856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R3JTH7; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000238064; 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: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:SF42; DNA TRANSLOCASE SFTA; 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:AVK62856.1};
KW   Cell division {ECO:0000313|EMBL:AVK62856.1};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}.
FT   DOMAIN          509..701
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          15..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         526..533
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   843 AA;  89291 MW;  7C965B16313984C9 CRC64;
     MTHYDGPAFY RKYHQLTTKK QPSPAVVEPT PPVDTPPISA PAAPVSTPAM PARSASSAPA
     TQRTHGIFHP SHVPAQLAPT AHSMGSVVST DQANYLEIEA SLHKAATSYL LFATATDIER
     ADTELAQLEP SPATAPVMSA APTVTLTPTS HAATVVFEPE QAVAVSRASV AVASSAPTVV
     FEPTHPIDLT DRVAPTTATS AVTPPVTVPS LDQVEQPATP EVAVPSSAVA SAVGTEVTVT
     SEVAAPQSVA TSAVTTVAPT STVTSAAAKP THGLGLSLDA IMTEEHNAQA DLALFKDEPS
     KQPAPITPVA EDDLYQPVGV AHPAVTSTPV TSQATTAPAP TSASVEADVT PVSAAHNGTS
     AAPVLANQEL AAYHLPPLDL LKAPVIPDES EMDDWIEGKA SALDESLDAF GVDANVVDWT
     IGPTVTQFQV KLARGVKVNK ITNLNDDLKL ALAAKDIRIE APIPGRNTVG IEIPNKKSRP
     VMLSEVLNSD KFRDSKSPLT VALGVDLFGQ PQVTDLRKMP HGLIAGATGS GKSVFINSIL
     VSLLYKANPQ EVKLLLIDPK AVELAPYDKV PHLLAPVISE PKAASAALKW VVDEMDNRYD
     KLAAGGARNI EQFNEMAVAH HEDGLKMPYI VIVIDELADL MMVASSEVQD YIARITQKAR
     AAGIHLLVAT QRPSVDVVTG LIKNNIPTRI AFMVASQIDS RTILDASGAE RLLGRGDMLY
     LGNGQSTPIR LQGTYVDSEI DDIAQFVREQ AAPHYEFQPD NLAKHEEVAK SQDDLMPEVL
     AYLAEEETVS TSKLQRTFSV GYNRAANIID DLEQRDYVSA AKGSKPRDVY FTADDLTNLQ
     ANS
//