COMFA_BACSU
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 03-AUG-2022, entry version 130.
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 similar
RT 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 subtilis
RT 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., 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 [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., Sloma A.,
RA 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., 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 driving
CC 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 mostly to
CC the cell poles during the development of competence. Colocalizes with
CC ComGA (PubMed:16009133). During competence a number of proteins (at
CC least CoiA, ComFA, ComGA, DprA, RecA and SsbB) are thought to
CC colocalize at the cell pole, in a disruption of comEC ComFA no longer
CC accumulates (PubMed:17630974). During development of competence ComGA
CC and presumably ComFA colocalize in discrete foci which accumulate at
CC the cell poles and then delocalize without the overall levels of
CC proteins decreasing, these processes are coincident with the timing of
CC transformability 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}.
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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 AlphaFoldDB; P39145; -.
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; BSU_35470.
DR GeneID; 938537; -.
DR KEGG; bsu:BSU35470; -.
DR PATRIC; fig|224308.179.peg.3838; -.
DR eggNOG; COG4098; Bacteria.
DR OMA; VDAFPYS; -.
DR PhylomeDB; P39145; -.
DR BioCyc; BSUB:BSU35470-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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 Gene3D; 3.40.50.300; -; 2.
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; Cytoplasm; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..463
FT /note="ComF operon protein 1"
FT /id="PRO_0000102199"
FT DOMAIN 133..285
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 317..463
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 233..236
FT /note="DEVD box"
FT BINDING 146..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
