P0A5U4 (RECA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein RecA

Alternative name(s):
Recombinase A

Cleaved into the following chain:

1. Endonuclease PI-MtuI
   EC=3.1.-.-
   Alternative name(s):
   Mtu RecA intein

Gene names

Name:	recA
Ordered Locus Names:	Rv2737c, MT2806
ORF Names:	MTV002.02c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	790 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP-Rule MF_00268 PI-MtuI is an endonuclease. HAMAP-Rule MF_00268
Subunit structure	Interacts with UvrD1 and UvrA. Ref.8
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00268.
Post-translational modification	This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation. HAMAP-Rule MF_00268
Sequence similarities	Belongs to the RecA family. Contains 1 DOD-type homing endonuclease domain.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Intron homing SOS response
Cellular component	Cytoplasm
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Autocatalytic cleavage Isopeptide bond Protein splicing Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SOS response Inferred from electronic annotation. Source: HAMAP UV protection Inferred from mutant phenotype Ref.1. Source: MTBBASE intein-mediated protein splicing Inferred from electronic annotation. Source: InterPro intron homing Inferred from electronic annotation. Source: UniProtKB-KW recombinational repair Inferred from mutant phenotype Ref.1. Source: MTBBASE response to antibiotic Inferred from expression pattern PubMed 18799471. Source: MTBBASE strand invasion Inferred from direct assay PubMed 10074373. Source: MTBBASE
Cellular_component	cytosol Inferred from direct assay PubMed 15525680. Source: MTBBASE
Molecular_function	ATP binding Inferred from direct assay PubMed 10074373Ref.10PubMed 11850426Ref.6. Source: MTBBASE DNA-dependent ATPase activity Inferred from direct assay PubMed 12853636. Source: MTBBASE damaged DNA binding Inferred from electronic annotation. Source: HAMAP endodeoxyribonuclease activity Inferred from direct assay PubMed 11850426. Source: MTBBASE magnesium ion binding Inferred from direct assay PubMed 12167644PubMed 12853636. Source: MTBBASE manganese ion binding Inferred from direct assay PubMed 11850426PubMed 12853636. Source: MTBBASE recombinase activity Inferred from direct assay PubMed 10074373. Source: MTBBASE single-stranded DNA binding Inferred from direct assay Ref.6. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 251

251

Protein RecA, 1st part HAMAP-Rule MF_00268

PRO_0000030269

Chain

252 – 691

440

Endonuclease PI-MtuI HAMAP-Rule MF_00268

PRO_0000030270

Chain

692 – 790

99

Protein RecA, 2nd part HAMAP-Rule MF_00268

PRO_0000030271

Regions

Domain

366 – 508

143

DOD-type homing endonuclease

Nucleotide binding

67 – 74

8

ATP By similarity

Amino acid modifications

Cross-link

762

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) HAMAP-Rule MF_00268

Natural variations

Natural variant

305

1

R → Q in strain: Canetti and SO93.

Natural variant

430

1

A → L in strain: Canetti and SO93.

Natural variant

434 – 435

2

QQ → RR in strain: Canetti and SO93.

Natural variant

438 – 439

2

IY → VH in strain: Canetti and SO93.

Secondary structure

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790

Helix Strand Turn

Details...

Helix

5 – 22

18

Helix

24 – 26

3

Helix

46 – 51

6

Beta strand

53 – 58

6

Beta strand

61 – 68

8

Helix

74 – 85

12

Turn

86 – 88

3

Beta strand

90 – 97

8

Helix

102 – 108

7

Helix

112 – 114

3

Beta strand

116 – 118

3

Helix

123 – 135

13

Beta strand

139 – 145

7

Helix

147 – 149

3

Helix

153 – 157

5

Helix

168 – 184

17

Turn

185 – 187

3

Beta strand

189 – 195

7

Helix

214 – 219

6

Beta strand

221 – 230

10

Beta strand

235 – 237

3

Beta strand

239 – 250

12

Beta strand

258 – 260

3

Turn

262 – 264

3

Beta strand

267 – 269

3

Helix

270 – 275

6

Beta strand

281 – 285

5

Beta strand

287 – 289

3

Beta strand

291 – 312

22

Beta strand

317 – 320

4

Beta strand

325 – 328

4

Beta strand

331 – 334

4

Helix

335 – 337

3

Beta strand

343 – 345

3

Beta strand

655 – 676

22

Turn

677 – 679

3

Beta strand

681 – 684

4

Beta strand

687 – 690

4

Beta strand

695 – 704

10

Turn

705 – 707

3

Helix

711 – 720

10

Turn

721 – 723

3

Beta strand

724 – 727

4

Beta strand

729 – 734

6

Beta strand

737 – 742

6

Helix

743 – 752

10

Helix

754 – 766

13

Sequences

	Sequence		Length	Mass (Da)
	P0A5U4 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: AD16340D2ED5E572	FASTA	790	85,389
	10 20 30 40 50 60 MTQTPDREKA LELAVAQIEK SYGKGSVMRL GDEARQPISV IPTGSIALDV ALGIGGLPRG 70 80 90 100 110 120 RVIEIYGPES SGKTTVALHA VANAQAAGGV AAFIDAEHAL DPDYAKKLGV DTDSLLVSQP 130 140 150 160 170 180 DTGEQALEIA DMLIRSGALD IVVIDSVAAL VPRAELEGEM GDSHVGLQAR LMSQALRKMT 190 200 210 220 230 240 GALNNSGTTA IFINQLRDKI GVMFGSPETT TGGKALKFYA SVRMDVRRVE TLKDGTNAVG 250 260 270 280 290 300 NRTRVKVVKN KCLAEGTRIF DPVTGTTHRI EDVVDGRKPI HVVAAAKDGT LHARPVVSWF 310 320 330 340 350 360 DQGTRDVIGL RIAGGAIVWA TPDHKVLTEY GWRAAGELRK GDRVAQPRRF DGFGDSAPIP 370 380 390 400 410 420 ADHARLLGYL IGDGRDGWVG GKTPINFINV QRALIDDVTR IAATLGCAAH PQGRISLAIA 430 440 450 460 470 480 HRPGERNGVA DLCQQAGIYG KLAWEKTIPN WFFEPDIAAD IVGNLLFGLF ESDGWVSREQ 490 500 510 520 530 540 TGALRVGYTT TSEQLAHQIH WLLLRFGVGS TVRDYDPTQK RPSIVNGRRI QSKRQVFEVR 550 560 570 580 590 600 ISGMDNVTAF AESVPMWGPR GAALIQAIPE ATQGRRRGSQ ATYLAAEMTD AVLNYLDERG 610 620 630 640 650 660 VTAQEAAAMI GVASGDPRGG MKQVLGASRL RRDRVQALAD ALDDKFLHDM LAEELRYSVI 670 680 690 700 710 720 REVLPTRRAR TFDLEVEELH TLVAEGVVVH NCSPPFKQAE FDILYGKGIS REGSLIDMGV 730 740 750 760 770 780 DQGLIRKSGA WFTYEGEQLG QGKENARNFL VENADVADEI EKKIKEKLGI GAVVTDDPSN 790 DGVLPAPVDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[4]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[5]	"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.
[6]	"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.
[7]	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.
[8]	"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.
[9]	"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.
[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X58485 Genomic DNA. Translation: CAA41395.1.
AJ000012 Genomic DNA. Translation: CAA03857.1.
AJ000011 Genomic DNA. Translation: CAA03856.1.
AE000516 Genomic DNA. Translation: AAK47127.1.
AL123456 Genomic DNA. Translation: CCP45535.1.

PIR

S18206.

RefSeq

NP_217253.1. NC_000962.3.
NP_337313.1. NC_002755.2.
YP_006516181.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G18	X-ray	3.80	A	1-790	[»]
1G19	X-ray	3.00	A	1-790	[»]
1MO3	X-ray	3.10	A	1-790	[»]
1MO4	X-ray	3.20	A	1-790	[»]
1MO5	X-ray	3.25	A	1-790	[»]
1MO6	X-ray	3.20	A	1-790	[»]
2IMZ	X-ray	1.70	A/B	253-691	[»]
2IN0	X-ray	1.60	A	252-691	[»]
2IN8	X-ray	1.70	A	252-691	[»]
2IN9	X-ray	1.80	A	252-691	[»]
2L8L	NMR	-	A	252-691	[»]
3IFJ	X-ray	1.90	A/B	252-691	[»]
3IGD	X-ray	2.40	A	252-691	[»]

ProteinModelPortal

P0A5U4.

SMR

P0A5U4. Positions 1-345, 589-769.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv2737c.

Protein family/group databases

MEROPS

N10.009.

Proteomic databases

PRIDE

P0A5U4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK47127; AAK47127; MT2806.

GeneID

13319464.
888371.
925483.

KEGG

mtc:MT2806.
mtu:Rv2737c.

PATRIC

18127918. VBIMycTub22151_3058.

Organism-specific databases

TubercuList

Rv2737c.

Phylogenomic databases

eggNOG

COG1372.

KO

K03553.

ProtClustDB

PRK09519.

Family and domain databases

Gene3D

3.10.28.10. 1 hit.
3.30.250.10. 1 hit.

HAMAP

MF_00268. RecA.

InterPro

IPR003593. AAA+_ATPase.
IPR013765. DNA_recomb/repair_RecA.
IPR020584. DNA_recomb/repair_RecA_CS.
IPR020588. DNA_recomb_RecA/RadB_ATP-bd.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR004042. Intein_endonuc.
IPR006141. Intein_splice_site.
IPR027417. P-loop_NTPase.
IPR023400. RecA_C.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]

PANTHER

PTHR22942:SF1. PTHR22942:SF1. 1 hit.

Pfam

PF00154. RecA. 2 hits.
[Graphical view]

PRINTS

PR00379. INTEIN.
PR00142. RECA.

SMART

SM00382. AAA. 1 hit.
SM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
SSF55608. SSF55608. 1 hit.

TIGRFAMs

TIGR01443. intein_Cterm. 1 hit.
TIGR01445. intein_Nterm. 1 hit.
TIGR02012. tigrfam_recA. 1 hit.

PROSITE

PS50818. 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]

ProtoNet

Search...

Other

BindingDB

P0A5U4.

ChEMBL

CHEMBL1741171.

EvolutionaryTrace

P0A5U4.

Entry information

Entry name

RECA_MYCTU

Accession

Primary (citable) accession number: P0A5U4
Secondary accession number(s): L0TAH5, O34519, P26345

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program