ID U5P4E3_9STRE Unreviewed; 754 AA.
AC U5P4E3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=N597_06540 {ECO:0000313|EMBL:AGY38614.1};
OS Streptococcus ilei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY38614.1, ECO:0000313|Proteomes:UP000017124};
RN [1] {ECO:0000313|EMBL:AGY38614.1, ECO:0000313|Proteomes:UP000017124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I-P16 {ECO:0000313|Proteomes:UP000017124};
RA Hyun D.-W.;
RT "Genome sequence of Streptococcus SP. I-P16 isolated from human ileal
RT fluid.";
RL Submitted (SEP-2013) 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; CP006776; AGY38614.1; -; Genomic_DNA.
DR AlphaFoldDB; U5P4E3; -.
DR STRING; 1156433.N597_06540; -.
DR KEGG; sip:N597_06540; -.
DR PATRIC; fig|1156433.3.peg.1278; -.
DR HOGENOM; CLU_001981_9_6_9; -.
DR Proteomes; UP000017124; 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 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:AGY38614.1};
KW Cell division {ECO:0000313|EMBL:AGY38614.1};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 418..614
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 435..442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 754 AA; 83026 MW; 83E383C041D11823 CRC64;
MILTIVLTLV FIFAFLRLGA LGIVTYNLIR LLVGSLAYVA MTAVIFHLFF FKWIEKHEGT
LSGFLSLFAG LLLMYQAYFV SLLKLEGSSV GPTLSRILGD LVHLRVSSFA GGGLLGAILY
TPVAFLLSNI GTYFIGGLLI LLGLLLMSSY SVYDVYEQAV AAFHSFMEKR EVRRQERFAE
REKKKALQAE AEEAARIEQL AEASPMSTEG YPVDLETGEV IEPEIEAEVP AEEAYPQIYL
PNEEEGYSED WPEDDPEEIE ELTEEDMDEE VTVDFTPKEL LQYKLPTIDL FAPDKPKNQS
KEKNIVRQNI RILEETFASF NIKATVERAE IGPSVTKYEV KPAVGVRVNR ISNLADDLAL
ALAAKDVRIE APIPGKSLVG IEVPNSEIAT VSFRELWEQS KTDPAKLLEI PLGKAVDGSA
RTFDLARMPH LLVAGSTGSG KSVAVNGIIS SILMKARPDE VKFMMVDPKM VELSVYNDIP
HLLIPVVTNP RKASRALQKV VDEMENRYEL FSKVGARNIA GFNAKVAEYN TQSEMKQVPL
PLIVVIVDEL ADLMMVASKE VEDAIIRLGQ KARAAGIHMI LATQRPSVDV ISGLIKANVP
SRVAFAVSSG TDSRTILDEN GAEKLLGRGD MLFKPIDENH PIRLQGSFIS DDDVERIVNF
VKEQAEADYD DAFDPGEVSE SDFDGGMGGS DEGDPLFEEA KALVIETQKA SASMIQRRLS
VGFNRATRLM EDLEAAGVIG PAEGTKPRKV LQTN
//
