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Protein

Protein RecA

Gene

recA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
PI-MtuI is an endonuclease.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 748ATPBy similarity

GO - Molecular functioni

  • ATPase activity Source: MTBBASE
  • ATP binding Source: MTBBASE
  • DNA-dependent ATPase activity Source: MTBBASE
  • double-stranded DNA binding Source: GO_Central
  • endodeoxyribonuclease activity Source: MTBBASE
  • four-way junction DNA binding Source: GO_Central
  • magnesium ion binding Source: MTBBASE
  • manganese ion binding Source: MTBBASE
  • recombinase activity Source: MTBBASE
  • single-stranded DNA binding Source: MTBBASE

GO - Biological processi

  • cellular response to DNA damage stimulus Source: MTBBASE
  • DNA recombinase assembly Source: GO_Central
  • intein-mediated protein splicing Source: InterPro
  • intron homing Source: UniProtKB-KW
  • mitotic recombination Source: GO_Central
  • recombinational repair Source: MTBBASE
  • response to antibiotic Source: MTBBASE
  • response to ionizing radiation Source: GO_Central
  • SOS response Source: UniProtKB-KW
  • strand invasion Source: MTBBASE
  • UV protection Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Intron homing, SOS response

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RecA
Alternative name(s):
Recombinase A
Cleaved into the following chain:
Alternative name(s):
Mtu RecA intein
Gene namesi
Name:recA
Ordered Locus Names:Rv2737c
ORF Names:MTV002.02c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2737c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1741171.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Protein RecA, 1st partPRO_0000030269Add
BLAST
Chaini252 – 691440Endonuclease PI-MtuIPRO_0000030270Add
BLAST
Chaini692 – 79099Protein RecA, 2nd partPRO_0000030271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki762 – 762Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Post-translational modificationi

This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.

Keywords - PTMi

Autocatalytic cleavage, Isopeptide bond, Protein splicing, Ubl conjugation

Proteomic databases

PaxDbiP9WHJ3.

Interactioni

Subunit structurei

Interacts with UvrD1 and UvrA.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2737c.

Chemistry

BindingDBiP9WHJ3.

Structurei

Secondary structure

1
790
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2218Combined sources
Helixi24 – 263Combined sources
Helixi46 – 516Combined sources
Beta strandi53 – 586Combined sources
Beta strandi61 – 688Combined sources
Helixi73 – 8614Combined sources
Beta strandi91 – 977Combined sources
Helixi102 – 1087Combined sources
Helixi112 – 1143Combined sources
Beta strandi116 – 1183Combined sources
Helixi123 – 13513Combined sources
Beta strandi140 – 1456Combined sources
Helixi147 – 1493Combined sources
Helixi153 – 1564Combined sources
Helixi167 – 18620Combined sources
Beta strandi189 – 1957Combined sources
Helixi213 – 2197Combined sources
Beta strandi221 – 23414Combined sources
Beta strandi237 – 25115Combined sources
Beta strandi258 – 2603Combined sources
Turni262 – 2643Combined sources
Beta strandi267 – 2693Combined sources
Helixi270 – 2756Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi291 – 31222Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi325 – 3284Combined sources
Beta strandi331 – 3344Combined sources
Helixi335 – 3373Combined sources
Beta strandi343 – 3475Combined sources
Turni349 – 3513Combined sources
Beta strandi655 – 67622Combined sources
Turni677 – 6793Combined sources
Beta strandi681 – 6844Combined sources
Beta strandi687 – 6904Combined sources
Beta strandi698 – 7047Combined sources
Turni705 – 7073Combined sources
Helixi711 – 72111Combined sources
Beta strandi724 – 7285Combined sources
Beta strandi731 – 7344Combined sources
Beta strandi737 – 7426Combined sources
Helixi743 – 75210Combined sources
Helixi754 – 76714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G18X-ray3.80A1-790[»]
1G19X-ray3.00A1-790[»]
1MO3X-ray3.10A1-790[»]
1MO4X-ray3.20A1-790[»]
1MO5X-ray3.25A1-790[»]
1MO6X-ray3.20A1-790[»]
2IMZX-ray1.70A/B252-691[»]
2IN0X-ray1.60A252-691[»]
2IN8X-ray1.70A252-691[»]
2IN9X-ray1.80A252-691[»]
2L8LNMR-A252-345[»]
A654-691[»]
3IFJX-ray1.90A/B252-691[»]
3IGDX-ray2.40A252-691[»]
4OQFX-ray2.80A1-771[»]
4PO1X-ray3.40A1-790[»]
4PO8X-ray2.70A1-790[»]
4PO9X-ray2.75A1-790[»]
4POAX-ray2.95A1-790[»]
4PPFX-ray2.30A1-790[»]
4PPGX-ray3.00A1-790[»]
4PPNX-ray2.60A1-790[»]
4PPQX-ray2.85A1-790[»]
4PQFX-ray2.80A1-790[»]
4PQRX-ray2.80A1-790[»]
4PQYX-ray2.95A1-790[»]
4PR0X-ray2.60A1-790[»]
4PSAX-ray2.65A1-790[»]
4PSKX-ray2.80A1-790[»]
4PSVX-ray2.60A1-790[»]
4PTLX-ray2.50A1-790[»]
ProteinModelPortaliP9WHJ3.
SMRiP9WHJ3. Positions 1-345, 589-772.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini366 – 508143DOD-type homing endonucleaseAdd
BLAST

Sequence similaritiesi

Belongs to the RecA family.Curated

Phylogenomic databases

eggNOGiCOG0468. LUCA.
COG1372. LUCA.
KOiK03553.
OMAiEICVEAM.
PhylomeDBiP9WHJ3.

Family and domain databases

Gene3Di2.170.16.10. 2 hits.
3.10.28.10. 1 hit.
3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00268. RecA.
InterProiIPR003593. AAA+_ATPase.
IPR013765. DNA_recomb/repair_RecA.
IPR020584. DNA_recomb/repair_RecA_CS.
IPR028992. Hedgehog/Intein_dom.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR030934. Intein_C.
IPR004042. Intein_endonuc.
IPR006141. Intein_N.
IPR004860. LAGLIDADG_2.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR023400. RecA_C.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERiPTHR22942:SF1. PTHR22942:SF1. 2 hits.
PfamiPF14528. LAGLIDADG_3. 1 hit.
PF00154. RecA. 1 hit.
[Graphical view]
PRINTSiPR00379. INTEIN.
PR00142. RECA.
SMARTiSM00382. AAA. 1 hit.
SM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]
SUPFAMiSSF51294. SSF51294. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
SSF55608. SSF55608. 1 hit.
TIGRFAMsiTIGR01443. intein_Cterm. 1 hit.
TIGR01445. intein_Nterm. 1 hit.
TIGR02012. tigrfam_recA. 1 hit.
PROSITEiPS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
PS00321. RECA_1. 1 hit.
PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WHJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQTPDREKA LELAVAQIEK SYGKGSVMRL GDEARQPISV IPTGSIALDV
60 70 80 90 100
ALGIGGLPRG RVIEIYGPES SGKTTVALHA VANAQAAGGV AAFIDAEHAL
110 120 130 140 150
DPDYAKKLGV DTDSLLVSQP DTGEQALEIA DMLIRSGALD IVVIDSVAAL
160 170 180 190 200
VPRAELEGEM GDSHVGLQAR LMSQALRKMT GALNNSGTTA IFINQLRDKI
210 220 230 240 250
GVMFGSPETT TGGKALKFYA SVRMDVRRVE TLKDGTNAVG NRTRVKVVKN
260 270 280 290 300
KCLAEGTRIF DPVTGTTHRI EDVVDGRKPI HVVAAAKDGT LHARPVVSWF
310 320 330 340 350
DQGTRDVIGL RIAGGAIVWA TPDHKVLTEY GWRAAGELRK GDRVAQPRRF
360 370 380 390 400
DGFGDSAPIP ADHARLLGYL IGDGRDGWVG GKTPINFINV QRALIDDVTR
410 420 430 440 450
IAATLGCAAH PQGRISLAIA HRPGERNGVA DLCQQAGIYG KLAWEKTIPN
460 470 480 490 500
WFFEPDIAAD IVGNLLFGLF ESDGWVSREQ TGALRVGYTT TSEQLAHQIH
510 520 530 540 550
WLLLRFGVGS TVRDYDPTQK RPSIVNGRRI QSKRQVFEVR ISGMDNVTAF
560 570 580 590 600
AESVPMWGPR GAALIQAIPE ATQGRRRGSQ ATYLAAEMTD AVLNYLDERG
610 620 630 640 650
VTAQEAAAMI GVASGDPRGG MKQVLGASRL RRDRVQALAD ALDDKFLHDM
660 670 680 690 700
LAEELRYSVI REVLPTRRAR TFDLEVEELH TLVAEGVVVH NCSPPFKQAE
710 720 730 740 750
FDILYGKGIS REGSLIDMGV DQGLIRKSGA WFTYEGEQLG QGKENARNFL
760 770 780 790
VENADVADEI EKKIKEKLGI GAVVTDDPSN DGVLPAPVDF
Length:790
Mass (Da):85,389
Last modified:April 16, 2014 - v1
Checksum:iAD16340D2ED5E572
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti305 – 3051R → Q in strain: Canetti and SO93.
Natural varianti430 – 4301A → L in strain: Canetti and SO93.
Natural varianti434 – 4352QQ → RR in strain: Canetti and SO93.
Natural varianti438 – 4392IY → VH in strain: Canetti and SO93.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58485 Genomic DNA. Translation: CAA41395.1.
AJ000012 Genomic DNA. Translation: CAA03857.1.
AJ000011 Genomic DNA. Translation: CAA03856.1.
AL123456 Genomic DNA. Translation: CCP45535.1.
PIRiS18206.
RefSeqiNP_217253.1. NC_000962.3.
WP_003414006.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45535; CCP45535; Rv2737c.
GeneIDi888371.
KEGGimtu:Rv2737c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58485 Genomic DNA. Translation: CAA41395.1.
AJ000012 Genomic DNA. Translation: CAA03857.1.
AJ000011 Genomic DNA. Translation: CAA03856.1.
AL123456 Genomic DNA. Translation: CCP45535.1.
PIRiS18206.
RefSeqiNP_217253.1. NC_000962.3.
WP_003414006.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G18X-ray3.80A1-790[»]
1G19X-ray3.00A1-790[»]
1MO3X-ray3.10A1-790[»]
1MO4X-ray3.20A1-790[»]
1MO5X-ray3.25A1-790[»]
1MO6X-ray3.20A1-790[»]
2IMZX-ray1.70A/B252-691[»]
2IN0X-ray1.60A252-691[»]
2IN8X-ray1.70A252-691[»]
2IN9X-ray1.80A252-691[»]
2L8LNMR-A252-345[»]
A654-691[»]
3IFJX-ray1.90A/B252-691[»]
3IGDX-ray2.40A252-691[»]
4OQFX-ray2.80A1-771[»]
4PO1X-ray3.40A1-790[»]
4PO8X-ray2.70A1-790[»]
4PO9X-ray2.75A1-790[»]
4POAX-ray2.95A1-790[»]
4PPFX-ray2.30A1-790[»]
4PPGX-ray3.00A1-790[»]
4PPNX-ray2.60A1-790[»]
4PPQX-ray2.85A1-790[»]
4PQFX-ray2.80A1-790[»]
4PQRX-ray2.80A1-790[»]
4PQYX-ray2.95A1-790[»]
4PR0X-ray2.60A1-790[»]
4PSAX-ray2.65A1-790[»]
4PSKX-ray2.80A1-790[»]
4PSVX-ray2.60A1-790[»]
4PTLX-ray2.50A1-790[»]
ProteinModelPortaliP9WHJ3.
SMRiP9WHJ3. Positions 1-345, 589-772.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2737c.

Chemistry

BindingDBiP9WHJ3.
ChEMBLiCHEMBL1741171.

Proteomic databases

PaxDbiP9WHJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45535; CCP45535; Rv2737c.
GeneIDi888371.
KEGGimtu:Rv2737c.

Organism-specific databases

TubercuListiRv2737c.

Phylogenomic databases

eggNOGiCOG0468. LUCA.
COG1372. LUCA.
KOiK03553.
OMAiEICVEAM.
PhylomeDBiP9WHJ3.

Miscellaneous databases

PROiP9WHJ3.

Family and domain databases

Gene3Di2.170.16.10. 2 hits.
3.10.28.10. 1 hit.
3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00268. RecA.
InterProiIPR003593. AAA+_ATPase.
IPR013765. DNA_recomb/repair_RecA.
IPR020584. DNA_recomb/repair_RecA_CS.
IPR028992. Hedgehog/Intein_dom.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR030934. Intein_C.
IPR004042. Intein_endonuc.
IPR006141. Intein_N.
IPR004860. LAGLIDADG_2.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR023400. RecA_C.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERiPTHR22942:SF1. PTHR22942:SF1. 2 hits.
PfamiPF14528. LAGLIDADG_3. 1 hit.
PF00154. RecA. 1 hit.
[Graphical view]
PRINTSiPR00379. INTEIN.
PR00142. RECA.
SMARTiSM00382. AAA. 1 hit.
SM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]
SUPFAMiSSF51294. SSF51294. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
SSF55608. SSF55608. 1 hit.
TIGRFAMsiTIGR01443. intein_Cterm. 1 hit.
TIGR01445. intein_Nterm. 1 hit.
TIGR02012. tigrfam_recA. 1 hit.
PROSITEiPS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
PS00321. RECA_1. 1 hit.
PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel structure of the recA locus of Mycobacterium tuberculosis implies processing of the gene product."
    Davis E.O., Sedgwick S.G., Colston M.J.
    J. Bacteriol. 173:5653-5662(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Vansoolingen D., Hoogenboezem T., Dehaas P.E., Hermans P.W.M.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canetti and SO93.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  4. "Protein splicing in the maturation of M. tuberculosis recA protein: a mechanism for tolerating a novel class of intervening sequence."
    Davis E.O., Jenner P.J., Brooks P.C., Colston M.J., Sedgwick S.G.
    Cell 71:201-210(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SPLICING.
  5. "Functional characterization of the precursor and spliced forms of RecA protein of Mycobacterium tuberculosis."
    Kumar R.A., Vaze M.B., Chandra N.R., Vijayan M., Muniyappa K.
    Biochemistry 35:1793-1802(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. Colston M.J., Davis E.O.
    (In) Bloom B.R. (eds.); Tuberculosis: pathogenesis, protection and control, pp.217-226, American Society for Microbiology, Washington D.C. (1994)
    Cited for: REVIEW.
  7. "Mycobacterium tuberculosis UvrD1 and UvrA proteins suppress DNA strand exchange promoted by cognate and noncognate RecA proteins."
    Singh P., Patil K.N., Khanduja J.S., Kumar P.S., Williams A., Rossi F., Rizzi M., Davis E.O., Muniyappa K.
    Biochemistry 49:4872-4883(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UVRD1 AND UVRA.
    Strain: ATCC 25618 / H37Rv.
  8. "Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis."
    Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H.
    PLoS ONE 5:E8589-E8589(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUPYLATION AT LYS-762, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: ATCC 25618 / H37Rv.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  10. "Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation."
    Datta S., Prabu M.M., Vaze M.B., Ganesh N., Chandra N.R., Muniyappa K., Vijayan M.
    Nucleic Acids Res. 28:4964-4973(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiRECA_MYCTU
AccessioniPrimary (citable) accession number: P9WHJ3
Secondary accession number(s): L0TAH5
, O34519, P0A5U4, P26345
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: June 8, 2016
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Intein-containing proteins
    List of intein-containing protein entries
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.