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Database: UniProt
Entry: V7HTM7_9LACO
LinkDB: V7HTM7_9LACO
Original site: V7HTM7_9LACO 
ID   V7HTM7_9LACO            Unreviewed;       695 AA.
AC   V7HTM7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Cell division protein {ECO:0000313|EMBL:ETA73574.1};
GN   ORFNames=LEQ_2414 {ECO:0000313|EMBL:ETA73574.1};
OS   Ligilactobacillus equi DPC 6820.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1392007 {ECO:0000313|EMBL:ETA73574.1, ECO:0000313|Proteomes:UP000018559};
RN   [1] {ECO:0000313|EMBL:ETA73574.1, ECO:0000313|Proteomes:UP000018559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 6820 {ECO:0000313|EMBL:ETA73574.1,
RC   ECO:0000313|Proteomes:UP000018559};
RX   PubMed=24435863;
RA   O'Donnell M.M., Harris H.M., O'Toole P.W., Ross R.P.;
RT   "The Genome of the Predominant Equine Lactobacillus Species, Lactobacillus
RT   equi, Is Reflective of Its Lifestyle Adaptations to an Herbivorous Host.";
RL   Genome Announc. 2:e01155-e01113(2014).
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:ETA73574.1}.
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DR   EMBL; AWWH01000173; ETA73574.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7HTM7; -.
DR   PATRIC; fig|1392007.3.peg.1620; -.
DR   Proteomes; UP000018559; 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: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   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; 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; 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:ETA73574.1};
KW   Cell division {ECO:0000313|EMBL:ETA73574.1};
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:UP000018559};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        86..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          358..555
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          144..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         375..382
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   695 AA;  75294 MW;  E121F4EAE275DC58 CRC64;
     MVTGHSPQLK NKRAFGGLVT YLGGLVTYEN FFLTQHKIDS DFLLRTMDAA MTNIQTNGSG
     NLVGGGIVGA GLYSISEFLV GPLGTYLVAG VVIILGLCLL AKIPLVTVLN FLSRLVKYLF
     QGVVALFKAT KAVSQKSKPL IENVQEKHQE RHVVKEKESV AEQTQQDVAP QVAPSALGAA
     IGDDKDLPKP RSLAESSWQD QTQTEEIKAE TTKPSFVGVN ENYQLPPLKL LSEVAKTDQS
     SEQKAMKQNR KVLEETLQSF GVDAKVVNTI LGPAVTKYEL HPAIGVKVSK IVNLSDDLAL
     ALAAKDLRIE APIPGKSLVG IEVPNQNVAT VSFKSIIAAQ KKDPTKPLEV PLGRDISGNL
     ITADLAKMPH LLIAGSTGSG KSVAINGIIT SLLMNTTPEQ VRLVLVDPKK VELGVYNDVA
     HLLTPVVTDP KKAAGALHKL VVEMERRYEV FADTGQRNIT GYNKMLARQK ADGLESEEQP
     MPYIVAIVDE LSDLMMTASN EVEDAIVRLA QMARAAGIHM ILATQRPSVD VITGLIKANV
     PSRMAFAVSS GTDSRTIIDQ YGAEKLLGRG DMLFLPMGQN KPIRVQGAFI SDEDVENVVG
     FIKDQQTVSY DQSMEISDQD MVGSSGAGDG KDELYSQVLE FIRLEQKCSI SLLQRRFKIG
     YNRAARIVDD LAQDGLIGPQ EGSKPRQVLL PPNQD
//
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