ID C3G9C4_BACTU Unreviewed; 1310 AA.
AC C3G9C4;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Cell divisionFtsK/SpoIIIE {ECO:0000313|EMBL:EEM69590.1};
GN ORFNames=bthur0009_44450 {ECO:0000313|EMBL:EEM69590.1};
OS Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM69590.1};
RN [1] {ECO:0000313|EMBL:EEM69590.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM69590.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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:EEM69590.1}.
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DR EMBL; ACNG01000100; EEM69590.1; -; Genomic_DNA.
DR RefSeq; WP_000888061.1; NZ_CM000754.1.
DR HOGENOM; CLU_001981_12_1_9; -.
DR Proteomes; UP000001380; Chromosome.
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 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:EEM69590.1};
KW Cell division {ECO:0000313|EMBL:EEM69590.1};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 974..1166
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 115..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 371..425
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 156..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 991..998
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1310 AA; 147284 MW; 085955F4B0754534 CRC64;
MLDWMKKLFN KEEEQTAMNK EVPKQVESQP KIPRVNHYTE AREAQMASRN AGKCRFPLVP
DNGFDEEDVI ETGRFEEQPV QAVTYENEPI QRGIKVERSR RQYVEKVVST YEEPEMQYEP
EREPVVKKAS TPAQESNRRP FRPTEMISPI YGYNRPSVEK KEEKQEEVKE REDLEISVEG
KSVVDAWLEK KGYTLSDFSE GQAPTSSSHR AANEQGERQY EESKKEEKSV VDQWLEKNGY
EIERQEPIVE EKEVVQEMSA PQEVPAAELL HETIAERMEG AKQESDVVDK NILQEELVDS
KVEHEDTILS EEIKRSTEIE QPTIEVEKQA PEESVIVKAE EKLEETIVVE IPEEVEVIAE
AEEREEVEVI AETEESEEVE VIAEIEELEE VEVVAETEEL EEVEVTAETE ELEEVEVIAE
TEESEEVEVI AETEAPEEVE PVALEEMQQE MVLNEAIEQK NEFIHVAVAD EQTKKDVQSF
ADVLIAEEQS VVEETPIVEE QPVAEEAPVV KEQSVVEEAP IVEEQPVAEE APVVEEQSVV
EEAPIVEEAP VVEGQSVVEE APIAEEQPVA EETSVVEEQP VAEETLIVEE APVVEGQSVV
EEAPIAEEQP VAEETSVVEE QPVAEEAPVV EEQPVVQKEE PKREKKRHVP FNVVMLKQDR
ARLMERHASR TNGMQSSMSE RVENKPVHQV EEQPQVEEKP MQQVVVEPQV EEKQMQQVVE
PQVEEKPMQQ VVVEPQVEEK LMQQVVVEPQ VEEKPMQQVV VEPQVEEKPM QQVVVEPQVE
EKPVQQVVEP QVEEVQPVQQ VVAEQVQKPI SSTEVEEKAY VVNQRENDVR NVLQTPPTYT
IPSLTLLSIP QQAALDNTEW LEEQKELLDT TFNNFHVGAH VINVSQGPAV TRFEVQPDPG
VKVNKITNLS DDIKLSLAAK DIRIEAPIPG KSAIGIEVPN KESKPVFLRE ILRSPVFTKS
ESPLTVALGL DISGDPIVTD IRKMPHGLIA GATGSGKSVC INAILTSILY KAKPHEVKLM
LIDPKMVELA PYNSVPHLVA PVITDVKAAT AALKWAVEEM ERRYELFAHA GARDLTRYNT
IVSGREIPGE TLPYIVIVID ELADLMMVAP GDVEEAICRI AQKARACGIH LLVATQRPSV
DVITGLIKSN IPTRIAFTVS SQVDSRTIID IGGAEKLLGR GDMLFLGNGT SKPVRVQGVY
VSDDEIEKTV DHVKKQMKPN YLFKQEDLLA KTEQAESEDE LFFEACQFVV EQGGASTSSV
QRKFRIGYNR AARLIEEMES QGIISEGRGT KPRDVLISED EFAAMQETNV
//
