ID U5SB50_9LACT Unreviewed; 1027 AA.
AC U5SB50;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=Q783_03225 {ECO:0000313|EMBL:AGY81313.1};
OS Carnobacterium inhibens subsp. gilichinskyi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY81313.1, ECO:0000313|Proteomes:UP000017469};
RN [1] {ECO:0000313|EMBL:AGY81313.1, ECO:0000313|Proteomes:UP000017469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN1359 {ECO:0000313|EMBL:AGY81313.1,
RC ECO:0000313|Proteomes:UP000017469};
RX PubMed=24285647;
RA Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT (DSM 27470T).";
RL Genome Announc. 1:e00985-13(2013).
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 ---------------------------------------------------------------------------
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; CP006812; AGY81313.1; -; Genomic_DNA.
DR RefSeq; WP_023177277.1; NC_022606.1.
DR AlphaFoldDB; U5SB50; -.
DR STRING; 1266845.Q783_03225; -.
DR KEGG; caw:Q783_03225; -.
DR PATRIC; fig|1266845.5.peg.587; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_12_2_9; -.
DR Proteomes; UP000017469; 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 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; IPR027856; DUF4573.
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; PF15140; DUF4573; 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:AGY81313.1};
KW Cell division {ECO:0000313|EMBL:AGY81313.1};
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 695..887
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 712..719
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1027 AA; 115918 MW; 041E5B1F2E533F5E CRC64;
MPKYDGPSYQ KDQDRQKKFK FPFYRDAQNV TNKEGSLKTS ALENEDSQSV NQNIKTNEKK
HGFDFTAFQK DNTSVRNYLS TIGKEEQMKQ SEIKKQKKQV EKRIKQTNYS KESLKHAATP
FQEGRSSTPF KVQKIPSPYY GFQDRATSKG KNNAIDYLKI TLALEKKPEQ FLLFEEYLLN
KIELPLEDKI KEIEAVEELE SVEELESVKE LEAVEKLESV KELESVKELE AVKELEAVKE
IEAVEELESV KELESVKELE SVKELESVEE LESIKELESV KELEAVKELE AVKEIEAVEE
LESVKELESV EELESIKELE SVEEIESVEA VEEIESVEEL EAVEELEIVQ ESEEEFIQEP
EIVQKAKEEP VIDPNLKEKK INDSRHINKK RRSLSRSLVG MIEDEQNVRL NRGKDVARYF
GEGKIASKKT SHPIHQSRVT NKPNIQTSEE IENMEMLAAL SRMNYLDKQA FPPETPETPE
TPETPETPET PETPINDCSL ENNSQSIVNI AEERFSTPEL ESRVQKEVET ITEVKDATEI
GFEIDSSIEE IDEIYDENYM FPSVDLLLRP VMLEPNAIDD WVLEQAEILN ETLDAFNIHA
QVIGWTIGPA VTQFELQLGR GVKVNKITNL SDDLKLSLAA KDIRIEAPIP GKSSVGIEIP
NKKSRPVMLS EVMESVEFKE STSPLTVAIG VNIAGEAVVS TIDKMPHGLI AGATGSGKSV
FINSLLVSLL YKATPSEVKL LLIDPKAVEL APYNEIPHLL SPVISEPKAA SEALKWAVNE
MEERYQKLAA AGVRNIQRFN EKAEEHEDFG LKMPYIVIVI DELADLMMVA SNDVQDSIAR
ITQKARAAGI HLIVATQRPS VDVITGTIKN NIPTRVAFMV SSQVDSRTIL DTGGAEKLLG
RGDMLFQENG SGRPIRVQGT YVEKEIERIV KHVKDQRSAN YLFEPESLMM KLESVEGKDE
LFEDVLPFIV SEGQVSASAL QRKFKIGFNR AANLIESLEN ENFISGHKGS KPREVFLTKA
DYEEKFL
//
