ID W9EKC3_9LACO Unreviewed; 706 AA.
AC W9EKC3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:ETO40134.1};
GN ORFNames=B808_901 {ECO:0000313|EMBL:ETO40134.1};
OS Fructilactobacillus florum 8D.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1221538 {ECO:0000313|EMBL:ETO40134.1, ECO:0000313|Proteomes:UP000019474};
RN [1] {ECO:0000313|EMBL:ETO40134.1, ECO:0000313|Proteomes:UP000019474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8D {ECO:0000313|EMBL:ETO40134.1,
RC ECO:0000313|Proteomes:UP000019474};
RA Kim E.B., Marco M.L.;
RT "Genome sequencing of Lactobacillus florum 8D.";
RL Submitted (AUG-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:ETO40134.1}.
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; ALXG01000038; ETO40134.1; -; Genomic_DNA.
DR RefSeq; WP_009166741.1; NZ_ALXG01000038.1.
DR AlphaFoldDB; W9EKC3; -.
DR PATRIC; fig|1221538.3.peg.910; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000019474; 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: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; 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; 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:ETO40134.1};
KW Cell division {ECO:0000313|EMBL:ETO40134.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000019474}.
FT DOMAIN 373..565
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 22..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 706 AA; 77367 MW; 5F3C1B8A154AB6AA CRC64;
MKHYDGPAFF RKYFDGKIPF QKPTESTGHA TSAFQSRRSP VPTTKPSSSF LKSTVAVPQN
DLVQQTAAFQ PHNHAGKRHY QGIKTTLSPR YQRAIQALTN DANLIWLTTE VSVTSKDQSG
NHLKWSKLPT TVSEKKPKLP ADLHENKNEN TVDNSSKSTP APTRRGLGHS LQEIFQDEDL
GAEKLALFSE RTPTSKQDAV MPTAEASKKA ALPPRTIDSN EISKPAKNPQ AVVSQAGKLP
SLKLLNPPVE LPEDEQDDWI LQQAEVLDRT LEAFHVSGKV VSWTNGPTVT EFQVKLALGV
KVNKITNLND DLKLALAAKD IRIEAPIPGK STVGIEIPNP QPRPVMLSEV LQASAFQTEQ
APNQIALGVS IAGNPVASDL TSMPHALIAG ATGSGKSVFI NSMLLSLLYH ATPQDLRMLL
IDPKAVELAP YEGIPHLLTP VISDPQEAAA ALKWVTEEMD QRYERLRAAG VRNLEQYNRQ
VKSTGHAADQ LPTILVVIDE LADLMMVAAG EVQDYIVRIT QKARAAGIHL VIATQRPSVD
VVTGTIKNNI PTRIAFMVAS QIDSRTIIDQ AGAERLLGRG DLLYLGNGAS KPERLQGAFV
TNAEVEKVTA AVRAEGPVHY EFDPRSLVKQ ADQATAHDEL WSECLRYLAD EKTVSTSKLQ
RVFSIGYNRA ASLIDDLEQH QLISEQRGAK PRDVYLTPEK LQQLNN
//
