ID A0A0F3RUH9_9LACO Unreviewed; 980 AA.
AC A0A0F3RUH9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=VC81_03555 {ECO:0000313|EMBL:KJW13550.1};
OS Levilactobacillus spicheri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW13550.1, ECO:0000313|Proteomes:UP000033491};
RN [1] {ECO:0000313|EMBL:KJW13550.1, ECO:0000313|Proteomes:UP000033491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP38 {ECO:0000313|EMBL:KJW13550.1,
RC ECO:0000313|Proteomes:UP000033491};
RA Zheng J., Ganezle M.;
RL Submitted (MAR-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:KJW13550.1}.
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DR EMBL; JZCR01000006; KJW13550.1; -; Genomic_DNA.
DR RefSeq; WP_045806772.1; NZ_JZCR01000006.1.
DR AlphaFoldDB; A0A0F3RUH9; -.
DR STRING; 216463.VC81_03555; -.
DR PATRIC; fig|216463.3.peg.2539; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000033491; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:SF42; DNA TRANSLOCASE SFTA; 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:KJW13550.1};
KW Cell division {ECO:0000313|EMBL:KJW13550.1};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 637..829
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 654..661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 980 AA; 104589 MW; 03660D23D88EB0B7 CRC64;
MEHYDGPAFY RKFPVKPTPV KREDPITERA ASQVKQRQRR NAQPEQRPVP PVTATPAPND
HPETPNQPAG NGSYRPFQVT EIPKQLHWSH RITSGRQRYQ RLIQQLKKSA DSFLLFAQPG
SQTSAAPSMT AEVATPSAES AVTPTAPAEP AAGTSAPAAQ TEVFQPDPNF DRSAVTTSSV
TATDHAPVVT PGRELMAEPA PTEVFYPESL TFEPTVPADS ADEPAATASA AEISVAEEET
AAQPVPFVTT EASEASSSTD ESASAAEPAP SEEPEPAVES ENSEQSEQSV TLASAEAPAD
TSTIAEHDLT AASADDQPAP TEDAPTTADE PSTPVRPTTT VDYLPVGTVP APQGRGGVTE
APATEASAEK TPSDPDVQRL LARAENVPTP TSEETPASLA EPASETTEAS LTTSAMDAET
STSAATVTSV ADPQPETPAP AATSAAPVPK AKAKPSRGLG HSLGDIMQEE GNEQRNLALF
ADAAPAPEST ATADDAPIRG YHFPDLSLLP KPVVPDEAAL DEWIEHQAEV LDTTLTAFHV
DAHVTDWTIG PTVTQFQIKL ALGVKVNKIT NLNDDLKLAL AAKDIRIEAP IPGKPTVGIE
IPNKKSRPVM LSEILNSPAF KKSESPLTVA LGVDLFGQPQ VTDLRKMPHG LIAGATGSGK
SVFINSLLLS ILYKANPRQV KLLLIDPKAV EMAPYDGLPH LLAPVISDPK AAAAALKWVV
TEMDERYEKL AAAGVRNIEQ FNDRADANDE PGLKMPYIVI IIDELADLMM MAASEVQDYI
VRITQKARAA GIHLLVATQR PSVDIVTGTI KNNIPTRIAF MVSSQIDSRT ILDTTGAESL
LGRGDMLYLG NGASQPMRLQ GAFVESEVDR VTDFVRTQGK PQYAFEPNGL LKQETAAENQ
DELLPKVLEY IAQEKTVSTS KLQRVFSIGY NRAANLIDDL EQHNYVSPQH GSKPREVYLT
PDDLGKDLPE PHDQGAPFSS
//