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 24-JAN-2024, entry version 106. DE RecName: Full=ATP-dependent DNA helicase PcrA; DE EC=5.6.2.4; DE AltName: Full=DNA 3'-5' helicase PcrA {ECO:0000305}; GN Name=pcrA; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillota; 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=Couples ATP hydrolysis with the unwinding of duplex DNA by CC translocating in the 3'-5' direction.; EC=5.6.2.4; 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=5.6.2.4; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10388562}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro. DR CDD; cd17932; DEXQc_UvrD; 1. DR CDD; cd18807; SF1_C_UvrD; 1. DR Gene3D; 1.10.10.160; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01073; pcrA; 1. DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1. DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1. DR Pfam; PF21196; PcrA_UvrD_tudor; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Isomerase; 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 //