Detailed information NTG0000115

Experimentally validated

Overview

• Name: recA
• Type: Machinery gene
• Locus tag: BSU_16940
• Genome accession: NC_000964
• Coordinates: 1764645..1765691 (+)
• Length: 348 a.a.
• NCBI ID: NP_389576.2
• Uniprot ID: P16971
• Organism: Bacillus subtilis subsp. subtilis str. 168
• Function: homologous recombination Homologous recombination

Function

RecA forms filaments on single-stranded DNA (ssDNA), which is essential for its roles in gene regulation and homologous recombination. These filaments facilitate the strand exchange process, allowing the incoming DNA to integrate into the bacterial genome. RecA is also involved in the SOS response, which is activated in response to DNA damage.

Genomic Context

Location: 1759645..1770691

Locus tag	Gene name	Coordinates (strand)	Size (bp)	Protein ID	Product	Description
BSU_16870 (BSU16870)	efpI	1759655..1760383 (+)	729	NP_389569.2	EF-P-5 aminopentanone reductase (EF-P repair enzyme), NADPH-dependent	-
BSU_16880 (BSU16880)	ymfJ	1760464..1760721 (+)	258	NP_389570.1	putative enzyme	-
BSU_16910 (BSU16910)	rodZ	1761707..1762573 (+)	867	NP_389573.3	cell shape determination factor	-
BSU_16920 (BSU16920)	pgsA	1762623..1763204 (+)	582	NP_389574.2	CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase	-
BSU_16930 (BSU16930)	cinA	1763222..1764472 (+)	1251	NP_389575.2	competence-damage inducible regulator	Machinery gene
BSU_16940 (BSU16940)	recA	1764645..1765691 (+)	1047	NP_389576.2	multifunctional SOS repair factor	Machinery gene
BSU_16950 (BSU16950)	pbpX	1765859..1767034 (+)	1176	NP_389577.1	penicillin-binding endopeptidase X (lysozyme resistance)	-
BSU_16960 (BSU16960)	rny	1767310..1768872 (+)	1563	NP_389578.1	endoribonuclease Y	-
BSU_16970 (BSU16970)	pdeB	1768941..1769735 (+)	795	NP_389579.2	2'3' and 3'5' cyclic nucleotide monophosphates phosphodiesterase involved in biofilm formation	-
BSU_16980 (BSU16980)	spoVS	1769935..1770195 (+)	261	NP_389580.1	regulator required for dehydratation of the spore core and assembly of the coat (stage V sporulation)	-

Regulatory network

Positive effect      

Negative effect

Regulator	Target	Regulation
recX	recA	negative effect

Sequence

Protein

• Length: 348 a.a.
• Molecular weight: 38059.21 Da
• Isoelectric Point: 4.7315

>NTDB_id=115 BSU_16940 NP_389576.2 1764645..1765691(+) (recA) [Bacillus subtilis subsp. subtilis str. 168]
MSDRQAALDMALKQIEKQFGKGSIMKLGEKTDTRISTVPSGSLALDTALGIGGYPRGRIIEVYGPESSGKTTVALHAIAE
VQQQGGQAAFIDAEHALDPVYAQKLGVNIEELLLSQPDTGEQALEIAEALVRSGAVDIVVVDSVAALVPKAEIEGDMGDS
HVGLQARLMSQALRKLSGAINKSKTIAIFINQIREKVGVMFGNPETTPGGRALKFYSSVRLEVRRAEQLKQGNDVMGNKT
KIKVVKNKVAPPFRTAEVDIMYGEGISKEGEIIDLGTELDIVQKSGSWYSYEEERLGQGRENAKQFLKENKDIMLMIQEQ
IREHYGLDNNGVVQQQAEETQEELEFEE

Nucleotide

• Length: 1047 bp

>NTDB_id=115 BSU_16940 NP_389576.2 1764645..1765691(+) (recA) [Bacillus subtilis subsp. subtilis str. 168]
ATGAGTGATCGTCAGGCAGCCTTAGATATGGCTCTTAAACAAATAGAAAAACAGTTCGGCAAAGGTTCCATTATGAAACT
GGGAGAAAAGACAGATACAAGAATTTCTACTGTACCAAGCGGCTCCCTCGCTCTTGATACAGCACTGGGAATTGGCGGAT
ATCCTCGCGGACGGATTATTGAAGTATACGGTCCTGAAAGCTCAGGTAAAACAACTGTGGCGCTTCATGCGATTGCTGAA
GTTCAGCAGCAGGGCGGACAAGCCGCGTTTATCGATGCGGAGCATGCGTTAGATCCGGTATACGCGCAAAAGCTCGGTGT
TAACATCGAAGAGCTTTTACTGTCTCAGCCTGACACAGGCGAGCAGGCGCTTGAAATTGCGGAAGCATTGGTTCGAAGCG
GGGCAGTTGACATTGTCGTTGTCGACTCTGTAGCCGCTCTCGTTCCGAAAGCGGAAATTGAAGGCGACATGGGAGATTCG
CATGTCGGTTTACAAGCACGCTTAATGTCTCAAGCGCTTCGTAAGCTTTCAGGGGCCATTAACAAATCGAAGACAATCGC
GATTTTCATTAACCAAATTCGTGAAAAAGTCGGTGTTATGTTCGGGAACCCGGAAACAACACCTGGCGGCCGTGCGTTGA
AATTCTATTCTTCCGTGCGTCTTGAAGTGCGCCGTGCTGAACAGCTGAAACAAGGCAACGACGTAATGGGGAACAAAACG
AAAATCAAAGTCGTGAAAAACAAGGTGGCTCCGCCGTTCCGTACAGCCGAGGTTGACATTATGTACGGAGAAGGCATTTC
AAAAGAAGGCGAAATCATTGATCTAGGAACTGAACTTGATATCGTGCAAAAAAGCGGTTCATGGTACTCTTATGAAGAAG
AGCGTCTTGGCCAAGGCCGTGAAAATGCAAAACAATTCCTGAAAGAAAATAAAGATATCATGCTGATGATCCAGGAGCAA
ATTCGCGAACATTACGGCTTGGATAATAACGGAGTAGTGCAGCAGCAAGCTGAAGAGACACAAGAAGAACTCGAATTTGA
AGAATAA

Domains

Predicted by InterproScan.

• recA bacterial DNA recombination protein (RecA) (7-267)

3D structure

• AlphaFold DB: P16971

Similar proteins

Only experimentally validated proteins are listed.

Protein	Organism	Identities (%)	Coverage (%)	Ha-value
recA	Latilactobacillus sakei subsp. sakei 23K	74.924	93.966	0.704
recA	Streptococcus pneumoniae D39	66.477	100	0.672
recA	Streptococcus pneumoniae R6	66.477	100	0.672
recA	Streptococcus pneumoniae Rx1	66.477	100	0.672
recA	Streptococcus pneumoniae TIGR4	66.477	100	0.672
recA	Streptococcus mutans UA159	66.092	100	0.661
recA	Streptococcus mitis SK321	65.994	99.713	0.658
recA	Streptococcus mitis NCTC 12261	68.788	94.828	0.652
recA	Streptococcus pyogenes NZ131	67.683	94.253	0.638
recA	Neisseria gonorrhoeae MS11	63.584	99.425	0.632
recA	Neisseria gonorrhoeae MS11	63.584	99.425	0.632
recA	Neisseria gonorrhoeae strain FA1090	63.584	99.425	0.632
recA	Lactococcus lactis subsp. cremoris KW2	65.758	94.828	0.624
recA	Helicobacter pylori 26695	63.081	98.851	0.624
recA	Helicobacter pylori strain NCTC11637	63.081	98.851	0.624
recA	Ralstonia pseudosolanacearum GMI1000	64.742	94.54	0.612
recA	Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819	63.914	95.335	0.609
recA	Riemerella anatipestifer ATCC 11845 = DSM 15868	63.609	95.335	0.606
recA	Glaesserella parasuis strain SC1401	60.58	99.138	0.601
recA	Vibrio cholerae O1 biovar El Tor strain E7946	60.465	98.851	0.598
recA	Vibrio cholerae strain A1552	60.465	98.851	0.598
recA	Acinetobacter baumannii D1279779	61.243	97.126	0.595
recA	Pseudomonas stutzeri DSM 10701	62.813	92.219	0.579
recA	Acinetobacter baylyi ADP1	62.422	92.529	0.578
recA	Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539	60.681	92.816	0.563

References

• [1]: Rubén Torres et al. (2023) Bacillus subtilis RadA/Sms-Mediated Nascent Lagging-Strand Unwinding at Stalled or Reversed Forks Is a Two-Step Process: RadA/Sms Assists RecA Nucleation, and RecA Loads RadA/Sms. International Journal of Molecular Sciences 24(5):4536. [PMID: 36901969]
• [2]: Rogelio Hernández-Tamayo et al. (2022) ATPase Activity of Bacillus subtilis RecA Affects the Dynamic Formation of RecA Filaments at DNA Double Strand Breaks. MSphere 7(6):e0041222. [PMID: 36321831]
• [3]: Rubén Torres et al. (2021) Bacillus subtilis RecA, DisA, and RadA/Sms Interplay Prevents Replication Stress by Regulating Fork Remodeling. Frontiers in Microbiology 12:766897. [PMID: 34880841]
• [4]: Hector Romero et al. (2020) Bacillus subtilis RarA Acts as a Positive RecA Accessory Protein. Frontiers in Microbiology 11:92. [PMID: 32117122]
• [5]: Fernando Santos-Escobar et al. (2019) Roles of Bacillus subtilis RecA, Nucleotide Excision Repair, and Translesion Synthesis Polymerases in Counteracting Cr(VI)-Promoted DNA Damage. Journal of Bacteriology 201(8):e00073-19. [PMID: 30745368]
• [6]: Begoña Carrasco et al. (2019) Bacillus subtilis MutS Modulates RecA-Mediated DNA Strand Exchange Between Divergent DNA Sequences. Frontiers in Microbiology 10:237. [PMID: 30814990]
• [7]: Rubén Torres et al. (2019) Bacillus subtilis RadA/Sms contributes to chromosomal transformation and DNA repair in concert with RecA and circumvents replicative stress in concert with DisA. DNA Repair 77:45-57. [PMID: 30877841]
• [8]: Rubén Torres et al. (2019) Bacillus subtilis DisA regulates RecA-mediated DNA strand exchange. Nucleic Acids Research 47(10):5141-5154. [PMID: 30916351]
• [9]: Rubén Torres et al. (2019) Bacillus subtilis RecA interacts with and loads RadA/Sms to unwind recombination intermediates during natural chromosomal transformation. Nucleic Acids Research 47(17):9198-9215. [PMID: 31350886]
• [10]: Ester Serrano et al. (2018) RecA Regulation by RecU and DprA During Bacillus subtilis Natural Plasmid Transformation. Frontiers in Microbiology 9:1514. [PMID: 30050509]
• [11]: Motohiro Akashi et al. (2017) Transposition of insertion sequence IS256Bsu1 in Bacillus subtilis 168 is strictly dependent on recA. Genes & Genetic Systems 92(2):59-71. [PMID: 28344191]
• [12]: Shimin Le et al. (2017) Bacillus subtilis RecA with DprA-SsbA antagonizes RecX function during natural transformation. Nucleic Acids Research 45(15):8873-8885. [PMID: 28911099]
• [13]: Fernando H Ramírez-Guadiana et al. (2016) The RecA-Dependent SOS Response Is Active and Required for Processing of DNA Damage during Bacillus subtilis Sporulation. PloS One 11(3):e0150348. [PMID: 26930481]
• [14]: Samuel Million-Weaver et al. (2015) Replication Restart after Replication-Transcription Conflicts Requires RecA in Bacillus subtilis. Journal of Bacteriology 197(14):2374-82. [PMID: 25939832]
• [15]: Begoña Carrasco et al. (2015) Bacillus subtilis RecO and SsbA are crucial for RecA-mediated recombinational DNA repair. Nucleic Acids Research 43(12):5984-97. [PMID: 26001966]
• [16]: Ignacija Vlašić et al. (2014) Bacillus subtilis RecA and its accessory factors, RecF, RecO, RecR and RecX, are required for spore resistance to DNA double-strand break. Nucleic Acids Research 42(4):2295-307. [PMID: 24285298]
• [17]: Paula P Cardenas et al. (2014) DNA double strand break end-processing and RecA induce RecN expression levels in Bacillus subtilis. DNA Repair 14:1-8. [PMID: 24373815]
• [18]: Tribhuwan Yadav et al. (2014) Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic recombination. The Journal of Biological Chemistry 289(40):27640-52. [PMID: 25138221]
• [19]: Tribhuwan Yadav et al. (2013) Bacillus subtilis DprA recruits RecA onto single-stranded DNA and mediates annealing of complementary strands coated by SsbB and SsbA. The Journal of Biological Chemistry 288(31):22437-50. [PMID: 23779106]
• [20]: Begoña Carrasco et al. (2008) Bacillus subtilis SsbA and dATP regulate RecA nucleation onto single-stranded DNA. DNA Repair 7(6):990-6. [PMID: 18472308]
• [21]: Candela Manfredi et al. (2008) Bacillus subtilis RecO nucleates RecA onto SsbA-coated single-stranded DNA. The Journal of Biological Chemistry 283(36):24837-47. [PMID: 18599486]
• [22]: Cristina Cañas et al. (2008) The RecU Holliday junction resolvase acts at early stages of homologous recombination. Nucleic Acids Research 36(16):5242-9. [PMID: 18684995]
• [23]: Lyle A Simmons et al. (2007) Replication is required for the RecA localization response to DNA damage in Bacillus subtilis. Proceedings of The National Academy of Sciences of The United States of America 104(4):1360-5. [PMID: 17229847]
• [24]: Isabelle Mortier-Barrière et al. (2007) A key presynaptic role in transformation for a widespread bacterial protein: DprA conveys incoming ssDNA to RecA. Cell 130(5):824-36. [PMID: 17803906]
• [25]: Begoña Carrasco et al. (2005) Bacillus subtilis RecU Holliday-junction resolvase modulates RecA activities. Nucleic Acids Research 33(12):3942-52. [PMID: 16024744]
• [26]: A Raymond-Denise et al. (1992) Expression of the Bacillus subtilis dinR and recA genes after DNA damage and during competence. Journal of Bacteriology 174(10):3171-6. [PMID: 1577687]