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Database: UniProt
Entry: P39145
LinkDB: P39145
Original site: P39145 
ID   COMFA_BACSU             Reviewed;         463 AA.
AC   P39145;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-OCT-2019, entry version 121.
DE   RecName: Full=ComF operon protein 1;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase ComFA;
GN   Name=comFA; Synonyms=comF1; OrderedLocusNames=BSU35470;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=168;
RX   PubMed=8412657; DOI=10.1111/j.1365-2958.1993.tb01674.x;
RA   Londono-Vallejo J.A., Dubnau D.;
RT   "comF, a Bacillus subtilis late competence locus, encodes a protein
RT   similar to ATP-dependent RNA/DNA helicases.";
RL   Mol. Microbiol. 9:119-131(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969505; DOI=10.1099/13500872-142-11-3079;
RA   Soldo B., Lazarevic V., Mauel C., Karamata D.;
RT   "Sequence of the 305 degrees-307 degrees region of the Bacillus
RT   subtilis chromosome.";
RL   Microbiology 142:3079-3088(1996).
RN   [3]
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   [4]
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=11918817; DOI=10.1046/j.1365-2958.2002.02833.x;
RA   Berka R.M., Hahn J., Albano M., Draskovic I., Persuh M., Cui X.,
RA   Sloma A., Widner W., Dubnau D.;
RT   "Microarray analysis of the Bacillus subtilis K-state: genome-wide
RT   expression changes dependent on ComK.";
RL   Mol. Microbiol. 43:1331-1345(2002).
RN   [5]
RP   INDUCTION.
RC   STRAIN=168 / CU741;
RX   PubMed=11948146; DOI=10.1128/jb.184.9.2344-2351.2002;
RA   Ogura M., Yamaguchi H., Kobayashi K., Ogasawara N., Fujita Y.,
RA   Tanaka T.;
RT   "Whole-genome analysis of genes regulated by the Bacillus subtilis
RT   competence transcription factor ComK.";
RL   J. Bacteriol. 184:2344-2351(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=168;
RX   PubMed=16009133; DOI=10.1016/j.cell.2005.04.035;
RA   Hahn J., Maier B., Haijema B.J., Sheetz M., Dubnau D.;
RT   "Transformation proteins and DNA uptake localize to the cell poles in
RT   Bacillus subtilis.";
RL   Cell 122:59-71(2005).
RN   [7]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=17630974; DOI=10.1111/j.1365-2958.2007.05799.x;
RA   Kramer N., Hahn J., Dubnau D.;
RT   "Multiple interactions among the competence proteins of Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 65:454-464(2007).
CC   -!- FUNCTION: Involved in transformation (competence for DNA uptake).
CC       Required for DNA uptake but not for binding. May provide the
CC       driving force for transport of DNA through an aqueous channel.
CC       {ECO:0000269|PubMed:8412657}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Localizes
CC       mostly to the cell poles during the development of competence.
CC       Colocalizes with ComGA (PubMed:16009133). During competence a
CC       number of proteins (at least CoiA, ComFA, ComGA, DprA, RecA and
CC       SsbB) are thought to colocalize at the cell pole, in a disruption
CC       of comEC ComFA no longer accumulates (PubMed:17630974). During
CC       development of competence ComGA and presumably ComFA colocalize in
CC       discrete foci which accumulate at the cell poles and then
CC       delocalize without the overall levels of proteins decreasing,
CC       these processes are coincident with the timing of transformability
CC       and the site of DNA uptake (PubMed:16009133).
CC       {ECO:0000269|PubMed:16009133, ECO:0000269|PubMed:17630974}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in cells competent for DNA
CC       transformation; that is 5-15% of the population (PubMed:11918817,
CC       PubMed:16009133, PubMed:17630974). {ECO:0000269|PubMed:11918817,
CC       ECO:0000269|PubMed:16009133, ECO:0000269|PubMed:17630974}.
CC   -!- INDUCTION: Expression activated by ComK (PubMed:11918817,
CC       PubMed:11948146). {ECO:0000269|PubMed:11918817,
CC       ECO:0000269|PubMed:11948146}.
CC   -!- DISRUPTION PHENOTYPE: Destabilization of ComGA (PubMed:17630974).
CC       {ECO:0000269|PubMed:17630974}.
CC   -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
DR   EMBL; Z18629; CAA79226.1; -; Genomic_DNA.
DR   EMBL; U56901; AAC44940.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15564.1; -; Genomic_DNA.
DR   PIR; G69602; G69602.
DR   RefSeq; NP_391427.1; NC_000964.3.
DR   RefSeq; WP_003243962.1; NZ_JNCM01000033.1.
DR   SMR; P39145; -.
DR   STRING; 224308.BSU35470; -.
DR   TCDB; 3.A.11.1.1; the bacterial competence-related dna transformation transporter (dna-t) family.
DR   PaxDb; P39145; -.
DR   PRIDE; P39145; -.
DR   EnsemblBacteria; CAB15564; CAB15564; BSU35470.
DR   GeneID; 938537; -.
DR   KEGG; bsu:BSU35470; -.
DR   PATRIC; fig|224308.179.peg.3838; -.
DR   eggNOG; COG4098; LUCA.
DR   HOGENOM; HOG000075153; -.
DR   KO; K02240; -.
DR   OMA; LSRDFSC; -.
DR   PhylomeDB; P39145; -.
DR   BioCyc; BSUB:BSU35470-MONOMER; -.
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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR   GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Competence; Complete proteome; Cytoplasm; Helicase;
KW   Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    463       ComF operon protein 1.
FT                                /FTId=PRO_0000102199.
FT   DOMAIN      133    285       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      317    463       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     146    153       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       233    236       DEVD box.
SQ   SEQUENCE   463 AA;  52566 MW;  69B719A504BE26BC CRC64;
     MNVPVEKNSS FSKELQQTLR SRHLLRTELS FSDEMIEWHI KNGYITAENS ISINKRRYRC
     NRCGQTDQRY FSFYHSSGKN KLYCRSCVMM GRVSEEVPLY SWKEENESNW KSIKLTWDGK
     LSSGQQKAAN VLIEAISKKE ELLIWAVCGA GKTEMLFPGI ESALNQGLRV CIATPRTDVV
     LELAPRLKAA FQGADISALY GGSDDKGRLS PLMISTTHQL LRYKDAIDVM IIDEVDAFPY
     SADQTLQFAV QKARKKNSTL VYLSATPPKE LKRKALNGQL HSVRIPARHH RKPLPEPRFV
     WCGNWKKKLN RNKIPPAVKR WIEFHVKEGR PVFLFVPSVS ILEKAAACFK GVHCRTASVH
     AEDKHRKEKV QQFRDGQLDL LITTTILERG VTVPKVQTGV LGAESSIFTE SALVQIAGRT
     GRHKEYADGD VIYFHFGKTK SMLDARKHIK EMNELAAKVE CTD
//
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