ID A0A0F4LQ49_9LACO Unreviewed; 758 AA.
AC A0A0F4LQ49;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN Name=ftsK {ECO:0000313|EMBL:KJY60932.1};
GN ORFNames=JG30_11200 {ECO:0000313|EMBL:KJY60932.1};
OS Bombilactobacillus mellifer.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1218492 {ECO:0000313|EMBL:KJY60932.1, ECO:0000313|Proteomes:UP000033558};
RN [1] {ECO:0000313|EMBL:KJY60932.1, ECO:0000313|Proteomes:UP000033558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin4 {ECO:0000313|EMBL:KJY60932.1,
RC ECO:0000313|Proteomes:UP000033558};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (JAN-2015) 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}.
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:KJY60932.1}.
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DR EMBL; JXJQ01000009; KJY60932.1; -; Genomic_DNA.
DR RefSeq; WP_046316926.1; NZ_KQ034028.1.
DR AlphaFoldDB; A0A0F4LQ49; -.
DR STRING; 1218492.JG30_11200; -.
DR PATRIC; fig|1218492.5.peg.1264; -.
DR HOGENOM; CLU_001981_9_6_9; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000033558; 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: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: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:KJY60932.1};
KW Cell division {ECO:0000313|EMBL:KJY60932.1};
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:UP000033558};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 62..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 417..615
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 229..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 435..442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 758 AA; 83924 MW; 04CBB477AF5516FF CRC64;
MSTKRKRKST KKTNKTTKKN KKYVLNFVGL VLVFISLFAG CKLGLAGRFL ANVYRVFVGD
SYLIVALLLA LLGIFLFLFG RVPHIGWKRT LGLAFLIIGS LTIMHGMLFQ QLNLKNDLIG
VTWRLLMNEM HNNQVANSVG GGLIGAFCLV WERPLLSIQG TYLINGLITL SGFLMLCQVQ
WQQVVNFCRT LVSWLVRLLH LLHWPKFKKR SPSQRAKSLV AKQPKISPVK SDSVTADDDF
TIEGPQPPVK SSTKSPKSST PPSSLTSSEK APITAKTSSD QEYQLPKIDL LTNVPPADQS
QEYELIDYNR KKLKQTFDSF GVQVDVKKAT LGPTVTKYEI QPAIGVKVSR IVNLADDLAL
ALAAKDIRIE APIPGKPYVG IEVPNQHASI VSFREVIEHE PAHPGEILTV PLGKDVYGQI
AMCNLVKMPH LLIAGSTGSG KSVAINTIIT GILMQARPSE VKMILIDPKM VELSVYNGIP
HLLIPVVTDV KKATGALQKA VDEMERRYRL FEKTGHRKIE EYNTAVDQNN QDPDNPPMDR
LPYIVVIVDE LSDLMMAAGK DVETSIVRLS QKARAAGMHL IIATQRPSVD VITGLIKANI
PSRMAFAVSS NIDSRTILDS TGAEKLLGRG DMLFLPLGAS KPQRIQGAYI SSQDVEQVVS
FVSSQQAAEY DETMIPSDQP DAKQNQDPDD AYWQQAVELV IHEQRASVSM LQRRFAIGYN
RAARLIDYME ERGLVGPARG SKPRKVLISR SEDDKQDD
//
