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Description:
Protein recA (Recombinase A).
Molecular weight: 37842
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
07-MAR-2006, entry version 13.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein RECA_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | V00328 | CAA23618.1 | - |
| EMBL | U00096 | AAC75741.1 | - |
| EMBL | D90892 | BAA16561.1 | - |
| PIR | G65049 | RQECA. | |
| PDB | 1AA3 | NMR | @=268-330. |
| PDB | 1N03 | EM | A/B/C/D/E/F/G=1-352. |
| PDB | 1REA | X-ray | @=1-352. |
| PDB | 1U94 | X-ray | A=1-352. |
| PDB | 1U98 | X-ray | A=1-352. |
| PDB | 1U99 | X-ray | A=1-352. |
| PDB | 1XMS | X-ray | A=1-352. |
| PDB | 1XMV | X-ray | A=1-352. |
| PDB | 2REB | X-ray | @=1-352. |
| PDB | 2REC | EM | A/B/C/D/E/F=1-352. |
| IntAct | P0A7G6 | -.1 | |
| SWISS-2DPAGE | P0A7G6 | COLI. | |
| ECO2DBASE | C039.3 | 6TH EDITION. | |
| GenomeReviews | U00096_GR | b2699.1 | |
| EchoBASE | EB0816 | -.1 | |
| EcoGene | EG10823 | recA. | |
| LinkHub | P0A7G6 | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| HAMAP | MF_00268 | - | 1. |
| InterPro | IPR003593 | AAA_ATPase. | |
| InterPro | IPR001553 | RecA_bac. | |
| Pfam | PF00154 | RecA | 1. |
| PRINTS | PR00142 | RECA. | |
| ProDom | PD000229 | RecA | 1. |
| SMART | SM00382 | AAA | 1. |
| TIGRFAMs | TIGR02012 | tigrfam_recA | 1. |
| PROSITE | PS00321 | RECA_1 | 1. |
| PROSITE | PS50162 | RECA_2 | 1. |
| PROSITE | PS50163 | RECA_3 | 1. |
Keywords:
3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; SOS response.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-5.
RX MEDLINE=80145618; PubMed=6244554;
RA Horii T., Ogawa T., Ogawa H.;
RT "Organization of the recA gene of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:313-317(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-2.
RX MEDLINE=80234673; PubMed=6930655;
RA Sancar A., Stachelek C., Konigsberg W., Rupp W.D.;
RT "Sequences of the recA gene and protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:2611-2615(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=91109725; PubMed=2274037;
RA Zhao X.J., McEntee K.;
RT "DNA sequence analysis of the recA genes from Proteus vulgaris,
RT Erwinia carotovora, Shigella flexneri and Escherichia coli B/r.";
RL Mol. Gen. Genet. 222:369-376(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [6]
RP PROTEIN SEQUENCE OF 89-106 AND 178-183.
RX MEDLINE=95255284; PubMed=7737176;
RA Morimatsu K., Horii T.;
RT "The DNA-binding site of the RecA protein. Photochemical cross-linking
RT of Tyr103 to single-stranded DNA.";
RL Eur. J. Biochem. 228:772-778(1995).
RN [7]
RP PROTEIN SEQUENCE OF 186-193.
RX MEDLINE=96067680; PubMed=7588783;
RA Gardner R.V., Voloshin O.N., Camerini-Otero R.D.;
RT "The identification of the single-stranded DNA-binding domain of the
RT Escherichia coli RecA protein.";
RL Eur. J. Biochem. 233:419-425(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX MEDLINE=92114994; PubMed=1731246; DOI=10.1038/355318a0;
RA Story R.M., Weber I.T., Steitz T.A.;
RT "The structure of the E. coli recA protein monomer and polymer.";
RL Nature 355:318-325(1992).
RN [9]
RP ERRATUM.
RA Story R.M., Weber I.T., Steitz T.A.;
RL Nature 355:567-567(1992).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX MEDLINE=97185905; PubMed=9033586;
RA Yu X., Egelman E.H.;
RT "The RecA hexamer is a structural homologue of ring helicases.";
RL Nat. Struct. Biol. 4:101-104(1997).
RN [11]
RP STRUCTURE OF ATP-BINDING FOLD.
RX MEDLINE=92115005; PubMed=1731253; DOI=10.1038/355374a0;
RA Story R.M., Steitz T.A.;
RT "Structure of the recA protein-ADP complex.";
RL Nature 355:374-376(1992).
Feature:
INIT_MET 0 0
CHAIN 1 352 Protein recA.
/FTId=PRO_0000122703.
NP_BIND 66 73 ATP.
CONFLICT 112 112 D -> E (in Ref. 5).
CONFLICT 190 190 Missing (in Ref. 7).
TURN 4 4
HELIX 5 21
HELIX 23 25
TURN 29 30
STRAND 39 40
HELIX 45 50
TURN 51 51
STRAND 56 57
TURN 58 59
STRAND 61 65
TURN 68 69
HELIX 72 85
TURN 86 87
STRAND 90 94
HELIX 101 106
TURN 107 108
HELIX 111 113
STRAND 115 117
HELIX 122 135
STRAND 140 144
HELIX 146 148
HELIX 152 155
HELIX 166 185
TURN 186 186
STRAND 188 193
HELIX 213 218
STRAND 221 233
TURN 234 235
STRAND 236 249
STRAND 257 263
TURN 264 266
STRAND 267 268
HELIX 270 280
TURN 281 282
STRAND 285 287
TURN 288 289
STRAND 290 293
TURN 294 295
STRAND 296 300
HELIX 301 311
HELIX 313 327
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.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: In response to low temperature. Sensitive to
temperature through changes in the linking number of the DNA.
-!- SIMILARITY: Belongs to the recA family.
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Sequence length: 352
AIDENKQKAL AAALGQIEKQ FGKGSIMRLG EDRSMDVETI STGSLSLDIA LGAGGLPMGR
IVEIYGPESS GKTTLTLQVI AAAQREGKTC AFIDAEHALD PIYARKLGVD IDNLLCSQPD
TGEQALEICD ALARSGAVDV IVVDSVAALT PKAEIEGEIG DSHMGLAARM MSQAMRKLAG
NLKQSNTLLI FINQIRMKIG VMFGNPETTT GGNALKFYAS VRLDIRRIGA VKEGENVVGS
ETRVKVVKNK IAAPFKQAEF QILYGEGINF YGELVDLGVK EKLIEKAGAW YSYKGEKIGQ
GKANATAWLK DNPETAKEIE KKVRELLLSN PNSTPDFSVD DSEGVAETNE DF