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Database: UniProt
Entry: A0A1H9PPI6_9LACT
LinkDB: A0A1H9PPI6_9LACT
Original site: A0A1H9PPI6_9LACT 
ID   A0A1H9PPI6_9LACT        Unreviewed;       833 AA.
AC   A0A1H9PPI6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=SAMN05421767_1662 {ECO:0000313|EMBL:SER50112.1};
OS   Granulicatella balaenopterae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Granulicatella.
OX   NCBI_TaxID=137733 {ECO:0000313|EMBL:SER50112.1, ECO:0000313|Proteomes:UP000198556};
RN   [1] {ECO:0000313|EMBL:SER50112.1, ECO:0000313|Proteomes:UP000198556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15827 {ECO:0000313|EMBL:SER50112.1,
RC   ECO:0000313|Proteomes:UP000198556};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOGF01000066; SER50112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9PPI6; -.
DR   STRING; 137733.SAMN05421767_1662; -.
DR   Proteomes; UP000198556; 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: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}; 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:UP000198556};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          477..678
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          222..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..828
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         499..506
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   833 AA;  93264 MW;  88CF062532571E0C CRC64;
     MSKKVKKKTS NKKKKKTNKE SNISIEVIGI IIIFISVIGV FRLGYIGLML TNLFRFFVGN
     STIIAFMIFI MYALYFIVKG KELEIPRNIF WSFLLAYITW LLMSDAMVFQ DIWQQNETPI
     GATLNNFASD FQQGQIETDM AGGIIGALLY TGSHFLFAQM GTYAVIIMLA ISSVLIFLQI
     GFSEVMVKVR ESLLDLADVF VREDNGDYQY EEDEKYIEAE KERKAKKKNK TKSEKKTPLK
     NVSSVGQSLK TRSKQFLDVI FDDEELEADK ANDGQQLDYE PELPIMDSFS DLEPFKDTYI
     PVEPPYPDFN ESEAHPAIKD NRNSEDASED TELGELNMGG TPEDDHYELP PLSLLNPVPV
     NDQTSEKNTV RKNMKILEQT FESFGVDCKV MDEPLLGPAV TKYEIKPAIG VKVSKIVNLS
     DDIALALAAK DIRIEAPIPG KPYVGIEVPN SKTSFVSFSD VIQASLLSPN KLDVPLGRDI
     SGNSRLCDLT RMPHMLIAGS TGSGKSVCIN GIITSILMKT KPHEVKLMMI DPKMVELNVY
     NGIPHLLTPV VTNPKKAAQA LQKVVAEMEK RYELFASMGM RNIDGYNQHV DQYNQEMGQN
     NPKLPYIVVI VDELADLMMV ASNEVEDAII RLAQMARAAG IHMILATQRP SVDVITGIIK
     ANVPSRIAFA VSSGTDSRTI IDANGAEKLL GRGDMLFMPM GENKPIRVQG AYITDEEVER
     VVEFVKNQQE VEYVEEMMPT DVPKQMDGEP EDELFGEALD LLKDLETVST SFLQRKFRIG
     YNRAARMIDE LEARGYIGPS EGSKPRKVNI QDFSEPEEKN ENAETLVEST KID
//
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