ID A0A147K9Q9_9BACI Unreviewed; 780 AA.
AC A0A147K9Q9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KUP07166.1};
GN ORFNames=Q75_06470 {ECO:0000313|EMBL:KUP07166.1};
OS Bacillus coahuilensis p1.1.43.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP07166.1, ECO:0000313|Proteomes:UP000074108};
RN [1] {ECO:0000313|EMBL:KUP07166.1, ECO:0000313|Proteomes:UP000074108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA Olmedo-Alvarez G.;
RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT Phosphorus Acquisition Strategies and Their Regulation.";
RL Front. Microbiol. 7:58-58(2016).
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:KUP07166.1}.
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DR EMBL; LDYG01000024; KUP07166.1; -; Genomic_DNA.
DR RefSeq; WP_059350790.1; NZ_LDYG01000024.1.
DR AlphaFoldDB; A0A147K9Q9; -.
DR STRING; 1150625.Q75_06470; -.
DR PATRIC; fig|1150625.3.peg.1352; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000074108; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF41; DNA TRANSLOCASE FTSK; 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:KUP07166.1};
KW Cell division {ECO:0000313|EMBL:KUP07166.1};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000074108};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 48..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 443..639
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 211..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 460..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 780 AA; 86773 MW; 03629E531B269509 CRC64;
MAKRKRRSRK KTMQLQTTIK FELIGIILIA LSIISIMEVG AVGKGLVLFA RFFFGEWFMI
LFAGAIVFAL YCMMKRQIPP LLTVRMMGIY LVLTALLLLS HVQLFQLLTN QGLVDTSVIR
NTWSLYWADV RGNVSTPDLG GGMIGAVLFA MSYYLFDNIG TQILSIIFIL IGFVLLTGKS
IGDFFGKILG GIRDFSVNQW QAFIQDAKDW KGQQSAKKEQ KKEKQREQRQ QEAENQSQVP
VIPQQDRPTM DDPSPEPIIS SFSQRNRDVT EEPTPLETVE EAPKDKENSS EEAVVVPMNF
NEVENESYEL PAIGILNSPS ETDQSNEYKL IHTNAAKLER TFQSFGVKAK VTQVHLGPAV
TKYEVHPDAG VKVSKIVGLT DDLALALAAK DIRIEAPIPG KSAIGIEVPN SEVAMVTLRE
VLEMYHHDKN SKLLIGLGRD IQGDAVTAEL NRMPHLLVAG ATGSGKSVCI NGIITSILMR
AKPHEVKLMM IDPKMVELNV YNGVPHLLAP VVTDPKKASQ ALKKVVNEME RRYELFSHTG
TRNIEGYNDH IKRHNAEHEE KQPELPFIVV IVDELADLMM VASNDVEDSI TRLAQMARAA
GIHLIIATQR PSVDVITGVI KANIPSRIAF AVSSQTDSRT ILDMGGAEKL LGKGDMLFFP
IGASKPVRVQ GAFLSDQEVE DIVDHVIEQQ KAQYQEEMIP SDVVDEPQEE VEDELYDDAV
QLVVEMQTAS VSMLQRRFRV GYTRAARLID AMELRGVVGP YEGSKPRQVL IQSINDEQTS
//
