ID A0A0R2IRJ4_9LACO Unreviewed; 638 AA.
AC A0A0R2IRJ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=IV80_GL000305 {ECO:0000313|EMBL:KRN67761.1};
OS Pediococcus cellicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=319652 {ECO:0000313|EMBL:KRN67761.1, ECO:0000313|Proteomes:UP000051568};
RN [1] {ECO:0000313|EMBL:KRN67761.1, ECO:0000313|Proteomes:UP000051568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17757 {ECO:0000313|EMBL:KRN67761.1,
RC ECO:0000313|Proteomes:UP000051568};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN67761.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQBR01000001; KRN67761.1; -; Genomic_DNA.
DR RefSeq; WP_057748460.1; NZ_JQBR01000001.1.
DR AlphaFoldDB; A0A0R2IRJ4; -.
DR STRING; 319652.IV80_GL000305; -.
DR PATRIC; fig|319652.3.peg.308; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000051568; 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: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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051568}.
FT DOMAIN 303..495
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 320..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 638 AA; 69986 MW; 90E31156B8F22942 CRC64;
MKHYDGPAFF RKDQEPKKQP VSRKRVKKHK SLNLDRQLTQ VPFFNADTDE SSKAELTTEL
PSDASTEKAV ATSAADHAKE ESANASVVPA ASDSIETESR ATPVGSAVNK ASQVDNEILR
SVKSQQIDHM SDPAFSSEQQ FEARQPVEPT ESARIQQAGL HKTSGTYQFP SLALLKSPVK
LDASSQSEWL QGQIKNLDEA LAAFGVDAKV VDWTVGPTVT QFQIELGRGV KVNKITNLTD
DLKLQLAAKD IRIEAPIPGK STVGIEIPNF KSRPVMLSEV LNSAVFKNSA SPLTIALGVD
LFGRPRVYDL RKMPHGLISG ATGSGKSVFI NSLLVSILYK ATPRQVRLLL IDPKTVELAP
YNELPHLLAP VISDPKAASA ALKWVTEEMD NRYERLAAAG VRNIEQFNKK AQTSGHEADS
LPYIVVIIDE LADLMMVAAS EVQDYIVRIT QKARAAGIHL VIATQRPSVD VVTGLIKNNI
PTRVAFMVSS QIDSRTILDH SGAERLLGRG DMLFLGNGAS TPIRLQGSYV DGEIDEITDF
IRSESQPHYA FDPNALKKEV EAVDDQDELM PEVLSYLADE DTISTSKLQR VFSIGYNHAA
TIIDQLEGQN YISEARGSKP REVYFTQADL KKIHDKPI
//
