ID A0A1B1Z6Z1_9BACI Unreviewed; 871 AA.
AC A0A1B1Z6Z1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=ABE41_014610 {ECO:0000313|EMBL:ANX13237.1};
OS Fictibacillus arsenicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX13237.1, ECO:0000313|Proteomes:UP000077412};
RN [1] {ECO:0000313|EMBL:ANX13237.1, ECO:0000313|Proteomes:UP000077412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-54 {ECO:0000313|EMBL:ANX13237.1,
RC ECO:0000313|Proteomes:UP000077412};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT toxicity to nematodes and a potential arsenic-resistance activity.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CP016761; ANX13237.1; -; Genomic_DNA.
DR RefSeq; WP_066291744.1; NZ_CP016761.1.
DR AlphaFoldDB; A0A1B1Z6Z1; -.
DR STRING; 255247.ABE41_014610; -.
DR KEGG; far:ABE41_014610; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000077412; Chromosome.
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: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; 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: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; 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}; 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:UP000077412}.
FT DOMAIN 534..726
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 14..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 551..558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 871 AA; 98385 MW; B89C57895BC70836 CRC64;
MSWIKKLMNT FFDDDNEDES LYEKEEQPVK KQRADEKGTP AHKPARTPAF KNSGRKPVQP
NNQHSAKMLH KYPENAPFRF PVIPDEKTSK KAPIQRNTYQ PRENNFEKEQ VVRREERSAR
SESRRSSSSM APNQKKPEPK RPAFKATHVP SPVYGYERKN KNSHKPTNDA KDSVSEVKSR
FTPTDVPSPV YGYGKRKPEG ILFIGRDIPP TNSIAEELLK SVDEALPAAP EEVVSVSEEI
RENAVLDPET PDEEFVDQEL IVHETRAAEH LIELEQEQEM ISEETPAFHQ EEAPVIFEDP
VQQEEKSNGL NEVSSTEAGP VQQERMEQER AGQEDTAPAP VIKRETPRSG GKYVPFNVLM
LKKDRQPSIS QTKKEQTTVR PQPPAFHTRP ERAVNENKQL FVPLSFLNKA AVSLEDDDIW
LNEQKHTLQS TLDNFNVNAK VVHMTKGPAV TRFEVQPAPG VKVNKITNLT DDIKLSLAAR
DIRIEAPIPG KNAIGIEVPN QHSRAVFLRE IIEHEVFRDS ASSLTVALGL DISGAPVVTD
LQKMPHGLIA GATGSGKSVC INSILVSLLY KAKPDEVRLL LVDPKMVELA PYNHIPHLVT
PVITDAKEAT AALKWAVEEM ERRYEEFAKT GVREIKRYNE KMEQERLYQN KMPYIVVVID
ELADLMMVSP QEVEEAICRI AQKARACGIH LLLATQRPSV DVITGLIKAN VPTRTAFAVS
SAIDSRTILD MSGAERLLGR GDMLFMENGS NKAVRIQGTF VSDEEIEEVT RYVKEEYKTD
YLFTREELIQ HQQTTEVEDE LFEEACYYVI EVGAASSSSL QRRFRIGYNR AARLVDMMES
FGLVSEAMGS KPRHVLLTQE ELENRLYSQV D
//
