ID A0A2T0BFH2_9CLOT Unreviewed; 796 AA.
AC A0A2T0BFH2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=DNA translocase SpoIIIE {ECO:0000313|EMBL:PRR82572.1};
GN Name=spoIIIE {ECO:0000313|EMBL:PRR82572.1};
GN ORFNames=CLVI_17070 {ECO:0000313|EMBL:PRR82572.1};
OS Clostridium vincentii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=52704 {ECO:0000313|EMBL:PRR82572.1, ECO:0000313|Proteomes:UP000239471};
RN [1] {ECO:0000313|EMBL:PRR82572.1, ECO:0000313|Proteomes:UP000239471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10228 {ECO:0000313|EMBL:PRR82572.1,
RC ECO:0000313|Proteomes:UP000239471};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium vincentii DSM 10228.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:PRR82572.1}.
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DR EMBL; PVXQ01000015; PRR82572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0BFH2; -.
DR Proteomes; UP000239471; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; 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; IPR025199; FtsK_4TM.
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:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF13491; FtsK_4TM; 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:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000239471};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 449..645
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 471..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 796 AA; 88096 MW; 60856078B7B8C3C4 CRC64;
MNRQNKRKNN KKSSDDDQTS KMEIKGIIII AIGLLSSIAI YTDLAGFLSS FAQKICHLLI
GIGSYILPIY LLYLGYNYFK GRGNISLGKN FHGLTIFIGV IILIFGTIYI QGKEVPNNFG
NNFMDLINAV ADGKRDLNGG VIGYVIAFPL YKFIGGLGSY ILYGALIIIS CILVFNFSPL
KAGQMAKIKG MEFREKEKAK KKVSENKNKN KNKDDYIKVL TKSDEVDKSK DEFLKGVNHK
IKILDFMKNS NVDEDSEFEL AIEENLDRPI SDFVDNMEFP ERTTKKGKLD NNIKDVVNKE
IDATISEGKE IQEIKEYIFP KIDLLNINGT TKLNSEDKKE LINSASKLEE ILGSFGVDAK
VAQVTKGPSV TRYEIQPSPG VKVSKIVNLA DDIALGLASS GVRIEAPIPG KAAVGIEVPN
KKQTPVFLRE VLDSNEFQNS TNKLAFALGK DIAGACVIGD LSKMPHTLIA GATGSGKSVC
INSLIISILY KYTPDEVKLL MVDPKVVELN VYNGIPHLLI PVVTDPKKAA AALNWAVNEM
TKRYNLFAEM GVRNIDSYNG LLDKGTIDKK LPYIVIIVDE LADLMMVCPN DVEDYIGRLA
QMARAAGMHL VIATQRPSVD VITGVIKANI PSRISFSVSS QVDSRTILDT GGAEKLLGKG
DMLYSPVGEN KPLRVQGCFI SEEEVESVVN FIKNDEKEII YEESIIEHIN KETDDKYVEE
GEDTDELLSE AVNLVVDFEQ ASISFIQRRL RVGFNRASRI MDQLEERGII SSKDGSRPRQ
VLVTKDQLIG NSQEDN
//
