Protein data for REP_ECOLI:

Description:
ATP-dependent DNA helicase rep (EC 3.6.1.-).

Molecular weight: 77024

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:
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 3.
07-MAR-2006, entry version 51.

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 REP_ECOLI:

Database Pointer Add. info#1 Add. info#2
EMBL X04794 CAA28481.1 ALT_FRAME
EMBL M87049 AAA67579.1 -
EMBL U00096 AAT48209.1 -
EMBL M11055 AAA24518.1 -
PIR E65181 HJECDR.
PDB 1UAA X-ray A/B=1-673.
GenomeReviews U00096_GR b3778.1
EchoBASE EB0830 -.1
EcoGene EG10837 rep.
BioCyc EcoCyc:EG10837-MONOMER -.1
LinkHub P09980 -.1
InterPro IPR005752 DNA_hel_RepA.
InterPro IPR000212 UvrD-helicase.
PANTHER PTHR11070 UvrD-helicase.1 1.
Pfam PF00580 UvrD-helicase 1.
TIGRFAMs TIGR01074 rep 1.

General information about the databases mentioned above

Keywords:
3D-structure; ATP-binding; Complete proteome; DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=87146372; PubMed=3029683;
RA Gilchrist C.A., Denhardt D.T.;
RT "Escherichia coli rep gene: sequence of the gene, the encoded
RT helicase, and its homology with uvrD.";
RL Nucleic Acids Res. 15:465-475(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=92358234; PubMed=1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region
RT from 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 196.
RA Arnaud M., Berlyn M.K.B., Blattner F.R., Galperin M.Y., Glasner J.D.,
RA Horiuchi T., Kosuge T., Mori H., Perna N.T., Plunkett G. III,
RA Riley M., Rudd K.E., Serres M.H., Thomas G.H., Wanner B.L.;
RT "Workshop on annotation of Escherichia coli K-12.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX MEDLINE=86059188; PubMed=2999067;
RA Bialkowska-Hobrzanska H., Gilchrist C.A., Denhardt D.T.;
RT "Escherichia coli rep gene: identification of the promoter and N
RT terminus of the rep protein.";
RL J. Bacteriol. 164:1004-1010(1985).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-640.
RX MEDLINE=97433075; PubMed=9288744; DOI=10.1016/S0092-8674(00)80525-5;
RA Korolev S., Hsieh J., Gauss G.H., Lohman T.M., Waksman G.;
RT "Major domain swiveling revealed by the crystal structures of
RT complexes of E. coli Rep helicase bound to single-stranded DNA and
RT ADP.";
RL Cell 90:635-647(1997).

Feature:
CHAIN 1 673 ATP-dependent DNA helicase rep.
/FTId=PRO_0000102068.
NP_BIND 22 29 ATP (By similarity).
CONFLICT 73 73 R -> H (in Ref. 1).
CONFLICT 76 76 A -> Q (in Ref. 1).
CONFLICT 163 165 IFA -> LLL (in Ref. 1).
CONFLICT 196 196 R -> A (in Ref. 2).
CONFLICT 202 203 KR -> NG (in Ref. 1).
HELIX 5 12
STRAND 15 20
TURN 24 25
STRAND 26 26
HELIX 28 43
HELIX 47 49
STRAND 50 56
HELIX 57 70
STRAND 71 71
TURN 73 78
STRAND 79 83
HELIX 84 98
TURN 99 100
STRAND 107 108
HELIX 110 120
TURN 121 121
STRAND 122 122
TURN 123 124
STRAND 125 125
STRAND 127 127
HELIX 129 143
TURN 144 146
TURN 149 150
HELIX 151 154
TURN 155 155
STRAND 158 158
HELIX 159 178
TURN 179 179
STRAND 181 182
HELIX 183 196
HELIX 198 205
TURN 206 207
STRAND 209 214
HELIX 216 218
STRAND 220 220
HELIX 221 231
TURN 232 234
STRAND 237 240
HELIX 243 245
HELIX 249 251
TURN 252 252
STRAND 253 253
TURN 255 256
HELIX 257 264
STRAND 265 265
TURN 266 267
STRAND 269 271
STRAND 276 279
HELIX 281 292
TURN 293 293
STRAND 294 294
STRAND 297 298
STRAND 304 306
STRAND 312 316
STRAND 318 319
HELIX 320 338
TURN 342 344
STRAND 345 352
HELIX 353 355
TURN 356 357
HELIX 358 364
TURN 365 366
STRAND 369 372
HELIX 377 379
HELIX 381 394
TURN 396 397
HELIX 399 405
STRAND 406 407
TURN 408 409
HELIX 415 427
TURN 428 429
STRAND 430 430
HELIX 432 435
TURN 436 437
TURN 439 440
HELIX 441 444
STRAND 445 445
STRAND 447 447
HELIX 448 467
TURN 468 469
HELIX 471 482
TURN 483 483
HELIX 484 491
STRAND 492 494
HELIX 495 516
TURN 517 517
STRAND 520 522
HELIX 527 535
TURN 536 537
STRAND 551 557
TURN 558 560
STRAND 561 562
STRAND 565 570
STRAND 574 576
TURN 577 580
HELIX 581 584
TURN 585 586
STRAND 587 587
HELIX 590 601
TURN 602 602
STRAND 603 611
STRAND 613 614
HELIX 617 619
STRAND 620 620
STRAND 626 626
HELIX 628 632
STRAND 633 633
TURN 635 637
STRAND 638 638

Comments:
-!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
involved in DNA replication; it can initiate unwinding at a nick
in the DNA. It binds to the single-stranded DNA and acts in a
progressive fashion along the DNA in the 3' to 5' direction.
-!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
-!- CAUTION: Ref.1 sequence differs from that shown in the C-terminus
and is shorter due to a frameshift.
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Sequence length: 673

     MRLNPGQQQA VEFVTGPCLV LAGAGSGKTR VITNKIAHLI RGCGYQARHI AAVTFTNKAA
     REMKERVGQT LGRKEARGLM ISTFHTLGLD IIKREYAALG MKANFSLFDD TDQLALLKEL
     TEGLIEDDKV LLQQLISTIS NWKNDLKTPS QAAASAIGER DRIFAHCYGL YDAHLKACNV
     LDFDDLILLP TLLLQRNEEV RKRWQNKIRY LLVDEYQDTN TSQYELVKLL VGSRARFTVV
     GDDDQSIYSW RGARPQNLVL LSQDFPALKV IKLEQNYRSS GRILKAANIL IANNPHVFEK
     RLFSELGYGA ELKVLSANNE EHEAERVTGE LIAHHFVNKT QYKDYAILYR GNHQSRVFEK
     FLMQNRIPYK ISGGTSFFSR PEIKDLLAYL RVLTNPDDDS AFLRIVNTPK REIGPATLKK
     LGEWAMTRNK SMFTASFDMG LSQTLSGRGY EALTRFTHWL AEIQRLAERE PIAAVRDLIH
     GMDYESWLYE TSPSPKAAEM RMKNVNQLFS WMTEMLEGSE LDEPMTLTQV VTRFTLRDMM
     ERGESEEELD QVQLMTLHAS KGLEFPYVYM VGMEEGFLPH QSSIDEDNID EERRLAYVGI
     TRAQKELTFT LCKERRQYGE LVRPEPSRFL LELPQDDLIW EQERKVVSAE ERMQKGQSHL
     ANLKAMMAAK RGK

Back

Database	Pointer	Add. info#1	Add. info#2
EMBL	X04794	CAA28481.1	ALT_FRAME
EMBL	M87049	AAA67579.1	-
EMBL	U00096	AAT48209.1	-
EMBL	M11055	AAA24518.1	-
PIR	E65181	HJECDR.
PDB	1UAA	X-ray	A/B=1-673.
GenomeReviews	U00096_GR	b3778.1
EchoBASE	EB0830	-.1
EcoGene	EG10837	rep.
BioCyc	EcoCyc:EG10837-MONOMER	-.1
LinkHub	P09980	-.1
InterPro	IPR005752	DNA_hel_RepA.
InterPro	IPR000212	UvrD-helicase.
PANTHER	PTHR11070	UvrD-helicase.1	1.
Pfam	PF00580	UvrD-helicase	1.
TIGRFAMs	TIGR01074	rep	1.