PCRA_GEOSE
ID PCRA_GEOSE Reviewed; 724 AA.
AC P56255;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP-dependent DNA helicase PcrA;
DE EC=3.6.4.12;
GN Name=pcrA;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP CHARACTERIZATION.
RX PubMed=9592155; DOI=10.1093/nar/26.11.2686;
RA Bird L.E., Brannigan J.A., Subramanya H.S., Wigley D.B.;
RT "Characterisation of Bacillus stearothermophilus PcrA helicase: evidence
RT against an active rolling mechanism.";
RL Nucleic Acids Res. 26:2686-2693(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=8934527; DOI=10.1038/384379a0;
RA Subramanya H.S., Bird L.E., Brannigan J.A., Wigley D.B.;
RT "Crystal structure of a DExx box DNA helicase.";
RL Nature 384:379-383(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=10199404; DOI=10.1016/s0092-8674(00)80716-3;
RA Velankar S.S., Soultanas P., Dillingham M.S., Subramanya H.S., Wigley D.B.;
RT "Crystal structures of complexes of PcrA DNA helicase with a DNA substrate
RT indicate an inchworm mechanism.";
RL Cell 97:75-84(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ATP.
RX PubMed=10388562; DOI=10.1006/jmbi.1999.2873;
RA Soultanas P., Dillingham M.S., Velankar S.S., Wigley D.B.;
RT "DNA binding mediates conformational changes and metal ion coordination in
RT the active site of PcrA helicase.";
RL J. Mol. Biol. 290:137-148(1999).
RN [5]
RP MUTAGENESIS.
RX PubMed=10454638; DOI=10.1093/nar/27.16.3310;
RA Dillingham M.S., Soultanas P., Wigley D.B.;
RT "Site-directed mutagenesis of motif III in PcrA helicase reveals a role in
RT coupling ATP hydrolysis to strand separation.";
RL Nucleic Acids Res. 27:3310-3317(1999).
CC -!- FUNCTION: DNA helicase. Has a broad nucleotide specificity, even being
CC able to hydrolyze ethenonucleotides, and is able to couple the
CC hydrolysis to unwinding of DNA substrates. It is a 3'-5' helicase but
CC at high protein concentrations it can also displace a substrate with a
CC 5' tail. Preferred substrate being one with both single and double-
CC stranded regions of DNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10388562}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR PDB; 1PJR; X-ray; 2.50 A; A=1-724.
DR PDB; 1QHG; X-ray; 2.50 A; A=1-724.
DR PDB; 1QHH; X-ray; 2.50 A; A=1-167, B=168-440, C=441-555, D=556-724.
DR PDB; 2PJR; X-ray; 2.90 A; A/F=1-548, B/G=556-650.
DR PDB; 3PJR; X-ray; 3.30 A; A=1-724.
DR PDB; 5DMA; X-ray; 1.53 A; A=673-724.
DR PDBsum; 1PJR; -.
DR PDBsum; 1QHG; -.
DR PDBsum; 1QHH; -.
DR PDBsum; 2PJR; -.
DR PDBsum; 3PJR; -.
DR PDBsum; 5DMA; -.
DR AlphaFoldDB; P56255; -.
DR SMR; P56255; -.
DR BRENDA; 3.6.4.12; 623.
DR EvolutionaryTrace; P56255; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01073; pcrA; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding.
FT CHAIN 1..724
FT /note="ATP-dependent DNA helicase PcrA"
FT /id="PRO_0000102050"
FT DOMAIN 10..289
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 290..569
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT REGION 652..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560,
FT ECO:0000269|PubMed:10388562"
FT BINDING 34..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560,
FT ECO:0000269|PubMed:10388562"
FT BINDING 287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10388562"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2PJR"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 169..186
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2PJR"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2PJR"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2PJR"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 329..344
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 390..403
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:2PJR"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 424..435
FT /evidence="ECO:0007829|PDB:2PJR"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:2PJR"
FT TURN 442..446
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 454..461
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 462..474
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 480..490
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 493..500
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 503..525
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 531..537
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 544..546
FT /evidence="ECO:0007829|PDB:2PJR"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:1PJR"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 588..591
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 594..608
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 611..625
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 636..640
FT /evidence="ECO:0007829|PDB:1PJR"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:1PJR"
FT STRAND 678..681
FT /evidence="ECO:0007829|PDB:5DMA"
FT TURN 682..684
FT /evidence="ECO:0007829|PDB:5DMA"
FT STRAND 685..694
FT /evidence="ECO:0007829|PDB:5DMA"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:5DMA"
FT STRAND 700..705
FT /evidence="ECO:0007829|PDB:5DMA"
FT TURN 706..709
FT /evidence="ECO:0007829|PDB:5DMA"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:5DMA"
FT STRAND 720..723
FT /evidence="ECO:0007829|PDB:5DMA"
SQ SEQUENCE 724 AA; 82488 MW; 6D20CA468BFB4291 CRC64;
MNFLSEQLLA HLNKEQQEAV RTTEGPLLIM AGAGSGKTRV LTHRIAYLMA EKHVAPWNIL
AITFTNKAAR EMRERVQSLL GGAAEDVWIS TFHSMCVRIL RRDIDRIGIN RNFSILDPTD
QLSVMKTILK EKNIDPKKFE PRTILGTISA AKNELLPPEQ FAKRASTYYE KVVSDVYQEY
QQRLLRNHSL DFDDLIMTTI QLFDRVPDVL HYYQYKFQYI HIDEYQDTNR AQYTLVKKLA
ERFQNICAVG DADQSIYRWR GADIQNILSF ERDYPNAKVI LLEQNYRSTK RILQAANEVI
EHNVNRKPKR IWTENPEGKP ILYYEAMNEA DEAQFVAGRI REAVERGERR YRDFAVLYRT
NAQSRVMEEM LLKANIPYQI VGGLKFYDRK EIKDILAYLR VIANPDDDLS LLRIINVPKR
GIGASTIDKL VRYAADHELS LFEALGELEM IGLGAKAAGA LAAFRSQLEQ WTQLQEYVSV
TELVEEVLDK SGYREMLKAE RTIEAQSRLE NLDEFLSVTK HFENVSDDKS LIAFLTDLAL
ISDLDELDGT EQAAEGDAVM LMTLHAAKGL EFPVVFLIGM EEGIFPHNRS LEDDDEMEEE
RRLAYVGITR AEEELVLTSA QMRTLFGNIQ MDPPSRFLNE IPAHLLETAS RRQAGASRPA
VSRPQASGAV GSWKVGDRAN HRKWGIGTVV SVRGGGDDQE LDIAFPSPIG IKRLLAKFAP
IEKV
