RECA_BACSU
ID RECA_BACSU Reviewed; 348 AA.
AC P16971;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268};
GN Synonyms=recE {ECO:0000303|PubMed:2115993}; OrderedLocusNames=BSU16940;
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 / YB886 / BG214;
RX PubMed=2115993; DOI=10.1093/nar/18.14.4249;
RA Stranathan M.C., Bayles K.W., Yasbin R.E.;
RT "The nucleotide sequence of the recE+ gene of Bacillus subtilis.";
RL Nucleic Acids Res. 18:4249-4249(1990).
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 TO 85-88.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-281.
RC STRAIN=PB1831;
RA de Rossi E.;
RT "Cloning of a putative mdr gene from Bacillus subtilis.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RC STRAIN=168;
RA Albertini A., Caldwell B., Caramori T., Errington J., Foulger D.,
RA Thomaides H., Williams A.;
RT "The genetic organisation of the recA chromosomal region in Bacillus
RT subtilis.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DEVELOPMENTAL STAGE, AND 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 [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND RECRUITMENT TO DNA
RP DOUBLE-STRAND BREAKS.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=16061691; DOI=10.1083/jcb.200412090;
RA Kidane D., Graumann P.L.;
RT "Dynamic formation of RecA filaments at DNA double strand break repair
RT centers in live cells.";
RL J. Cell Biol. 170:357-366(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=16385024; DOI=10.1128/jb.188.2.353-360.2006;
RA Sanchez H., Kidane D., Castillo Cozar M., Graumann P.L., Alonso J.C.;
RT "Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the
RT absence of DNA end processing.";
RL J. Bacteriol. 188:353-360(2006).
RN [9]
RP SUBCELLULAR LOCATION.
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).
RN [10]
RP FUNCTION, INTERACTION WITH DPRA, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=17803906; DOI=10.1016/j.cell.2007.07.038;
RA Mortier-Barriere I., Velten M., Dupaigne P., Mirouze N., Pietrement O.,
RA McGovern S., Fichant G., Martin B., Noirot P., Le Cam E., Polard P.,
RA Claverys J.P.;
RT "A key presynaptic role in transformation for a widespread bacterial
RT protein: DprA conveys incoming ssDNA to RecA.";
RL Cell 130:824-836(2007).
RN [11]
RP FUNCTION, SUBUNIT, MODULATION BY RECU, AND INTERACTION WITH RECU.
RX PubMed=18684995; DOI=10.1093/nar/gkn500;
RA Canas C., Carrasco B., Ayora S., Alonso J.C.;
RT "The RecU Holliday junction resolvase acts at early stages of homologous
RT recombination.";
RL Nucleic Acids Res. 36:5242-5249(2008).
RN [12]
RP FUNCTION.
RX PubMed=25138221; DOI=10.1074/jbc.m114.577924;
RA Yadav T., Carrasco B., Serrano E., Alonso J.C.;
RT "Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic
RT recombination.";
RL J. Biol. Chem. 289:27640-27652(2014).
CC -!- FUNCTION: Multifunctional protein involved in homologous recombination,
CC DNA repair and competence (PubMed:16061691, PubMed:16385024,
CC PubMed:17803906, PubMed:18684995, PubMed:25138221). Can catalyze the
CC hydrolysis of (d)ATP in the presence of single-stranded DNA; prefers
CC dATP at least in vitro, catalyzes the dATP-dependent uptake of single-
CC stranded DNA by duplex DNA, and the dATP-dependent hybridization of
CC homologous single-stranded DNAs (strand exchange) (PubMed:25138221).
CC RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA
CC activate strand exchange by RecA-ATP (PubMed:25138221). It interacts
CC with LexA causing its activation and leading to its autocatalytic
CC cleavage. Hydrolysis of ATP in the presence of single-stranded DNA is
CC partially inhibited by RecU (PubMed:18684995). Required for DNA
CC transformation; protects transforming DNA from degradation, possibly in
CC combination with DprA (PubMed:17803906). {ECO:0000269|PubMed:16061691,
CC ECO:0000269|PubMed:16385024, ECO:0000269|PubMed:18684995,
CC ECO:0000269|PubMed:25138221, ECO:0000305|PubMed:17803906}.
CC -!- FUNCTION: Recruited to repair centers (RCs), foci that are the site of
CC double-stranded DNA break(s), after RecN (PubMed:16061691). Concomitant
CC with the appearance of RecO at the RCs, RecA forms threads that extend
CC from RCs toward the opposite cell half, possibly searching for sequence
CC homology along the sister chromosome. The threads disappear after about
CC 2 hours (PubMed:16061691). Thread formation is absolutely dependent on
CC RecJ or AadAB (PubMed:16385024). {ECO:0000269|PubMed:16061691,
CC ECO:0000269|PubMed:16385024}.
CC -!- SUBUNIT: Monomer; forms higher-order oligomers (PubMed:16061691).
CC Interacts with RecU (PubMed:18684995). Interacts with DprA (smf)
CC (PubMed:17803906). {ECO:0000269|PubMed:17803906,
CC ECO:0000269|PubMed:18684995}.
CC -!- INTERACTION:
CC P16971; P39813: dprA; NbExp=3; IntAct=EBI-1535844, EBI-1535559;
CC P16971; P37475: spoIIE; NbExp=2; IntAct=EBI-1535844, EBI-9304781;
CC P16971; P37562: yabT; NbExp=2; IntAct=EBI-1535844, EBI-9303331;
CC P16971; P96715: ywqC; NbExp=3; IntAct=EBI-1535844, EBI-9302918;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000269|PubMed:16061691}. Note=Protein is recruited to RC foci
CC following DNA damage (PubMed:16061691). During competence a number of
CC proteins (at least CoiA, ComFA, ComGA, DprA, RecA and SsbB) are thought
CC to colocalize at the cell pole (PubMed:17630974).
CC {ECO:0000269|PubMed:17630974}.
CC -!- DEVELOPMENTAL STAGE: Induced during competence (PubMed:11948146).
CC {ECO:0000269|PubMed:11948146}.
CC -!- INDUCTION: By competence, expression activated by ComK
CC (PubMed:11948146). By DNA damage. {ECO:0000269|PubMed:11948146}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are extremely sensitive
CC to DNA-damaging agents. They show 4-fold impaired growth in their
CC absence. {ECO:0000269|PubMed:16385024}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; X52132; CAA36377.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13567.2; -; Genomic_DNA.
DR EMBL; U87792; AAB47709.1; -; Genomic_DNA.
DR EMBL; U56238; AAB00569.1; -; Genomic_DNA.
DR PIR; S10370; RQBSEE.
DR RefSeq; NP_389576.2; NC_000964.3.
DR RefSeq; WP_003245789.1; NZ_JNCM01000035.1.
DR RefSeq; WP_009967282.1; NZ_CM000487.1.
DR AlphaFoldDB; P16971; -.
DR SMR; P16971; -.
DR BioGRID; 857087; 1.
DR IntAct; P16971; 7.
DR MINT; P16971; -.
DR STRING; 224308.BSU16940; -.
DR jPOST; P16971; -.
DR PaxDb; P16971; -.
DR PRIDE; P16971; -.
DR EnsemblBacteria; CAB13567; CAB13567; BSU_16940.
DR GeneID; 939497; -.
DR KEGG; bsu:BSU16940; -.
DR PATRIC; fig|224308.179.peg.1835; -.
DR eggNOG; COG0468; Bacteria.
DR InParanoid; P16971; -.
DR OMA; DYGEQAL; -.
DR PhylomeDB; P16971; -.
DR BioCyc; BSUB:BSU16940-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00268; RecA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Competence; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Nucleotide-binding; Reference proteome;
KW SOS response.
FT CHAIN 1..348
FT /note="Protein RecA"
FT /id="PRO_0000122656"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT CONFLICT 85..88
FT /note="GGQA -> RTS (in Ref. 1; CAA36377 and 4; AAB47709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38059 MW; EE558B6354119260 CRC64;
MSDRQAALDM ALKQIEKQFG KGSIMKLGEK TDTRISTVPS GSLALDTALG IGGYPRGRII
EVYGPESSGK TTVALHAIAE VQQQGGQAAF IDAEHALDPV YAQKLGVNIE ELLLSQPDTG
EQALEIAEAL VRSGAVDIVV VDSVAALVPK AEIEGDMGDS HVGLQARLMS QALRKLSGAI
NKSKTIAIFI NQIREKVGVM FGNPETTPGG RALKFYSSVR LEVRRAEQLK QGNDVMGNKT
KIKVVKNKVA PPFRTAEVDI MYGEGISKEG EIIDLGTELD IVQKSGSWYS YEEERLGQGR
ENAKQFLKEN KDIMLMIQEQ IREHYGLDNN GVVQQQAEET QEELEFEE
