ID A0A428J8B0_9BACI Unreviewed; 824 AA.
AC A0A428J8B0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:RSK28210.1};
GN ORFNames=EJF36_15685 {ECO:0000313|EMBL:RSK28210.1};
OS Bacillus sp. HMF5848.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2495421 {ECO:0000313|EMBL:RSK28210.1, ECO:0000313|Proteomes:UP000274811};
RN [1] {ECO:0000313|EMBL:RSK28210.1, ECO:0000313|Proteomes:UP000274811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF5848 {ECO:0000313|EMBL:RSK28210.1,
RC ECO:0000313|Proteomes:UP000274811};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Bacillus sp. HMF5848 Genome sequencing and assembly.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:RSK28210.1}.
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DR EMBL; RWIV01000001; RSK28210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428J8B0; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000274811; Unassembled WGS sequence.
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 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: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:UP000274811}.
FT DOMAIN 487..679
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 504..511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 824 AA; 93222 MW; C7D24FF768DCC5E3 CRC64;
MNWFRKLFST PEDENYNNLN KEPEKMRNEN EKASVKMAYE YPKGTFRFPI IPDEEPGVMH
DKHKSKSKSK DLKQQKEYTQ PYQAVNVNKH AQAQKKEKKS FKRTEVPSPI YGFAPRKQTN
TEDEYFKKDN KEKDFEDFDT QRLENVVSSF QENKHTQDNV QIESEVKLKI SEEKQIHHNE
KEDFVNHEED NNTQHFVEFE PEPSTDTLNN AANNDADDTT ANSDVDELID DVTIADKYYE
NEKEQTEPEL TQAPVLKQET ESENEGTSPA RMFSNSMDES SDVNHLNHGT NEITQDDGLN
EEETHTTNNE EGKHTTSRPR AIPYNVIMLK KDRESINQRT SRPSEQNQHD SYKFPSLNTL
TAAPVNTEGD AEWINNQRVL LEETLFNFNV RANVVNVTQG PAVTRFEVQP EPGVKVNKIT
NLSDDIKLSL SAKDIRIEAP IPGKNTIGIE VPNRTSKPVF LREILEAAVF KESSSPLTVA
MGLDIAGNPI VTDIHKMPHG LIAGATGSGK SVCINTMLVS LIYKAKPQDV RLLLIDPKMV
ELAPYNNIPH LASPVITDVK AATAALKWAV EEMERRYELF AHAGVRDIKR FNELAREKGK
REEHLPYLVI IIDELADLMM VAPGDVEEAI ARIAQKARAC GIHLLVATQR PSVDVITGLI
KANIPTRVAF SVSSQVDSRT IIDISGAEKL LGKGDMLFLE NGASKPVRLQ GCFVNDQEID
EIVSFAKKQG SPNFMFTQEE MLKKTIESPQ MDDELYTEAC EFVLEQGGAS TSSLQRRFRI
GYNRAARLID MMEEQGIISE NRGSKPRDIL IDETELAEKL ETQQ
//