ID A0A024QAG5_9BACI Unreviewed; 809 AA.
AC A0A024QAG5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Septum-associated FtsK-like translocase of DNA {ECO:0000313|EMBL:CDQ39282.1};
GN Name=sftA {ECO:0000313|EMBL:CDQ39282.1};
GN ORFNames=BN990_01576 {ECO:0000313|EMBL:CDQ39282.1};
OS Virgibacillus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ39282.1, ECO:0000313|Proteomes:UP000028875};
RN [1] {ECO:0000313|EMBL:CDQ39282.1, ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ39282.1,
RC ECO:0000313|Proteomes:UP000028875};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL Submitted (MAY-2014) 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:CDQ39282.1}.
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DR EMBL; CCDP010000001; CDQ39282.1; -; Genomic_DNA.
DR RefSeq; WP_038243232.1; NZ_CCDP010000001.1.
DR AlphaFoldDB; A0A024QAG5; -.
DR STRING; 1462526.BN990_01576; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000028875; 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:UP000028875}.
FT DOMAIN 477..669
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 16..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 494..501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 809 AA; 92603 MW; 00785ABE6BD73155 CRC64;
MWDHWKQKIK SLFAESEIEE QQEENHKTEK SNLEAKMMYQ YPTNKSFRFP VIPDQAEQRK
ENTRKKNRNS VKTNNHNFMN NNLNEDRSSR IEPEQQQQSS VRLEKKNMEN SEELPAYQRK
RSRRSNSDRS TYHTSHSLSQ EEGRNVEREQ SANKVYKKDP DVPFKPTEVP SPIYGFRPRD
EQKAKVENIP AYQRKVDEKN KEPFSSEINQ EIRKESVEIA EREIAAETKE EEKVSELLHE
ENATPASVNI SEVKDSSKQQ PRKSEETENC SISEDRRRSS KRVNQREHKK QERQSGRATI
PFNVMMTPRD KKNLMEKSKK AKRRESEQKS EITKQELFNK KDTSIPYYLL DDIDRTNADD
DHWVQQQQQL LEQTLKHFNV RAKVVNATQG PSVTRFEVQP ELGVKVSKVK NLSDDLKLNM
AARDIRIEAP IPGKNTIGIE IPNRKAQMVG LQGIFETDAF KRNTSPLTIA LGLSIEGQPL
ITNIQKMPHG LIAGATGSGK SVCINTILIS LLYKASHEEV KFLLIDPKMV ELAPYNGIPH
LVSPVITDVK AATAALKWAV TEMEDRYEKF VHEGVRDIER YNQKMDKQQR TQDKLPFIVI
VIDELADLMM VSPQDVEDAI SRIAQKARAC GIHLLLATQR PSVDVITGLI KANIPTRIAF
SVSSQVDSRT ILDTSGAEKL LGKGDMLFIE NGAGKSMRLQ GPFVSDEEIE RVTNYTRSIA
EPNYLFEQEE LLEQVAMDEE EDDHLKDAVK FVLEQNGAST SLLQRHFKIG YNRAARLIDS
LEQRGIISGQ NGSKPREVLV TASQVEEML
//
