SFTA_BACSU
ID SFTA_BACSU Reviewed; 952 AA.
AC C0SP86; O34749; O34884; Q795T4; Q795T5;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=DNA translocase SftA;
DE AltName: Full=Septum-associated FtsK-like translocase of DNA;
GN Name=sftA; Synonyms=ytpS, ytpT; OrderedLocusNames=BSU29805;
GN ORFNames=BSU29810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION AS A DNA TRANSLOCASE, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=19788545; DOI=10.1111/j.1365-2958.2009.06893.x;
RA Biller S.J., Burkholder W.F.;
RT "The Bacillus subtilis SftA (YtpS) and SpoIIIE DNA translocases play
RT distinct roles in growing cells to ensure faithful chromosome
RT partitioning.";
RL Mol. Microbiol. 74:790-809(2009).
RN [5]
RP FUNCTION, DNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF LYS-645.
RC STRAIN=168 / PY79;
RX PubMed=19818024; DOI=10.1111/j.1365-2958.2009.06894.x;
RA Kaimer C., Gonzalez-Pastor J.E., Graumann P.L.;
RT "SpoIIIE and a novel type of DNA translocase, SftA, couple chromosome
RT segregation with cell division in Bacillus subtilis.";
RL Mol. Microbiol. 74:810-825(2009).
CC -!- FUNCTION: Required for the accurate completion of chromosome
CC partitioning, in part by promoting efficient resolution of chromosome
CC dimers, before the formation of the division septum. Binds to DNA in a
CC non-specific manner. Shows ATPase activity. Not required for
CC cytokinesis. {ECO:0000269|PubMed:19788545,
CC ECO:0000269|PubMed:19818024}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:19818024}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19788545,
CC ECO:0000269|PubMed:19818024}. Note=Colocalizes with FtsZ at nascent
CC division sites.
CC -!- DISRUPTION PHENOTYPE: Delay in chromosome segregation and an increase
CC in the sensitivity to agents that induce DNA damage. They divide over
CC unsegregated chromosomes with increased frequencies. A cell
CC filamentation phenotype can also be seen, when associated with a noc
CC deletion. {ECO:0000269|PubMed:19788545, ECO:0000269|PubMed:19818024}.
CC -!- MISCELLANEOUS: StfA and SpoIIIE are not functionally redundant. They
CC probably play distinct roles during growth and sporulation.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00292.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC00293.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF008220; AAC00292.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF008220; AAC00293.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB14959.2; -; Genomic_DNA.
DR PIR; B69999; B69999.
DR PIR; C69999; C69999.
DR RefSeq; NP_390859.2; NC_000964.3.
DR RefSeq; WP_003229272.1; NZ_CP053102.1.
DR AlphaFoldDB; C0SP86; -.
DR SMR; C0SP86; -.
DR STRING; 224308.BSU29805; -.
DR TCDB; 3.A.12.1.5; the septal dna translocator (s-dna-t) family.
DR PRIDE; C0SP86; -.
DR EnsemblBacteria; CAB14959; CAB14959; BSU_29805.
DR GeneID; 938522; -.
DR KEGG; bsu:BSU29805; -.
DR PATRIC; fig|224308.179.peg.3238; -.
DR eggNOG; COG1674; Bacteria.
DR InParanoid; C0SP86; -.
DR OMA; MMEAEGM; -.
DR PhylomeDB; C0SP86; -.
DR BioCyc; BSUB:BSU29805-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; 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; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..952
FT /note="DNA translocase SftA"
FT /id="PRO_0000389651"
FT DOMAIN 622..813
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 15..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 639..646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 645
FT /note="K->A: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:19818024"
SQ SEQUENCE 952 AA; 106823 MW; D0B21EE077D21DED CRC64;
MSWLHKFFDL FLGESEEDAE RETKPAQIPQ QQEVHHPEGQ LKRLEDPKIY YEYPKGKFRF
PVVPDGYKNH DLRRRRTPSD EPKSAPRPSA APYRERPRNE EEQHTYQAAE PAKKPFKPTN
IPSPVYGFNQ KPSVKKDVPK KPSETLNEPD KSVKEKVTLL SEEIERERGY PASDTQAHSK
IESPFFPDTQ FEKQPSGVLN RKDTEHDEAL AKRPAEPSGN KVPFESGVQQ PEKEEPFFPA
EQAEEQTPPE MLTDTAAEGL SDSEVGREEP ATAEEEQREQ QPEKFEEPVF SAELDEEQTA
PESQTEAVSE DEKAKEPSDS PVYNHHENAA EGAESPFVQE EQMDIRQEEP LFTDHEYSSE
ALAQAETVAK ESEEPSESII NNHYDTLGEA QETKIDVQPD SHTELEKTEH MEQGSKSSTA
TLENRQEIRA DKPREASEEP KKRPGVQEKR TEQSASSQKG PSVPFNVMML KRDTHKQQKA
EERRGSYVFP NVALLDVPPA QVQDDTAWIE EQRQLLDLTL KNFNVRANVV HVTQGPSVTR
FEVHPEPGVK VNKITNLSDD IKLSLSAKDI RIEAPIPGKN TIGIEVPNRT SKVVDLRQMI
RSSAFRTSKS PLTAALGLDI SGNPVVIDLK KMPHGLIAGA TGSGKSVCIN TILVSLLYKA
DPSEVKVLLI DPKMVELAPY NKIPHLVSPV ITDAKAATAA LKWVVEEMER RYELFAHSGV
RDIDRFNQLT AEHQMGEKLP YLVVIIDELA DLMMVAPNDV EESIARIAQK ARACGIHLLV
ATQRPSVDVI TGLIKANIPT RIAFSVSSQV DSRTIIDIAG AEKLLGKGDM LFLENGSGKP
VRLQGNFVSD REIDRVVSHV RSQMPPTYLF EQEELVRQGS ALKEEDELFY EACEFVVEQN
SASTSSLQRR FRIGYNRAAR LIDMMEAEGM ISEAKGSKPR EVLITASDLI NE
