ID I7LEP7_9LACO Unreviewed; 821 AA.
AC I7LEP7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=BN53_07555 {ECO:0000313|EMBL:CCI85933.1};
OS Lactobacillus pasteurii DSM 23907 = CRBIP 24.76.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423790 {ECO:0000313|EMBL:CCI85933.1, ECO:0000313|Proteomes:UP000009311};
RN [1] {ECO:0000313|EMBL:CCI85933.1, ECO:0000313|Proteomes:UP000009311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.76T {ECO:0000313|Proteomes:UP000009311};
RA Cousin S., Bouchier C., Loux V., Ma L., Creno S., Bizet C., Clermont D.;
RT "Draft Genome Sequence of Lactobacillus pasteurii CRBIP 24.76T.";
RL Submitted (JUN-2012) 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:CCI85933.1}.
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DR EMBL; CAKD01000024; CCI85933.1; -; Genomic_DNA.
DR RefSeq; WP_009560496.1; NZ_CAKD01000024.1.
DR AlphaFoldDB; I7LEP7; -.
DR STRING; 1423790.BN53_07555; -.
DR PATRIC; fig|1423790.3.peg.530; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000009311; 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; IPR036259; MFS_trans_sf.
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; SSF103473; MFS general substrate transporter; 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:CCI85933.1};
KW Cell division {ECO:0000313|EMBL:CCI85933.1};
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:UP000009311};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 477..674
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 494..501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 821 AA; 91238 MW; CE2E5E45F466CF2F CRC64;
MPKKKTSRNV KKRKNTVARK AKKKQEDTLY WVTSGIAMLV LSLLSFMRVG WLGKTVANLL
RFFVGDSYLI FAGIIAIVGT IMIIYGKLPK FRLKRGLGIV LILYPILLIQ SIGFFSKNLV
YSGFVNSFIT EIGEEFGRIN ITQSVGGGLF GAIAYQLLYP LLGQLGTTIL AWVLIPIGIL
MFLDVKYRTV VEKFQKSSQT FIDKNKEAGV KIKDKYTELR EQQQEARLQK EQENQANLRD
PFMDSNAVFP DVTDFSVDES DKQDEDQEDI PVVEATPSEP VQVQVAQQHE EAEEVQEDEE
PDELPRPHNF AQEDQKLVAE LADVNHGELD QQPAAKPNRI YKKPPLSLLD PIKKIDQSSD
KKMIQQNTAT LQSTFKSFGV DVIIKKAILG PTITRYEVQP AVGVKVSRIV NLADDLALAL
AAKDIRIEAP IPGKPFIGIE VPNKTTSAVS FKDVMEHQDA KGKQDPLTVP LGKDVTGQII
SANLTKMPHL LIAGSTGSGK SVAINTILTS ILMKARPEEV KLVLIDPKMV ELSVYNGVAH
LLIPVVTDSK LAAKALHKAV KEMERRYKLF AASGARNIGE YNQKVEENNQ DRSKPAMKPL
PFIVVVVDEL SDLMMVGGRE VEDQIVRLGQ MARAAGIHMI LATQRPSVDV ITGLIKANVP
SRISFAVSSG TDSRTILDQT GAEKLLGRGD MLYMPIGASK PERIQGAYIA SDEVEKVIEW
VKQQQEAEYD QEMIPQHGSS SDDSDNDEPE DEFYQQAVDL VRHQQSASVS MLQRRFRIGY
NRAARIVEEM EARGVVGPSE GSKPRQVLLP PEKEENHDAH N
//
