REP_BUCBP
ID REP_BUCBP Reviewed; 670 AA.
AC Q89A21;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000255|HAMAP-Rule:MF_01920};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01920};
GN Name=rep {ECO:0000255|HAMAP-Rule:MF_01920}; OrderedLocusNames=bbp_540;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
CC involved in DNA replication; it can initiate unwinding at a nick in the
CC DNA. It binds to the single-stranded DNA and acts in a progressive
CC fashion along the DNA in the 3' to 5' direction. {ECO:0000255|HAMAP-
CC Rule:MF_01920}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01920};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01920}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01920}.
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DR EMBL; AE016826; AAO27239.1; -; Genomic_DNA.
DR RefSeq; WP_011091640.1; NC_004545.1.
DR AlphaFoldDB; Q89A21; -.
DR SMR; Q89A21; -.
DR STRING; 224915.bbp_540; -.
DR PRIDE; Q89A21; -.
DR EnsemblBacteria; AAO27239; AAO27239; bbp_540.
DR GeneID; 56471074; -.
DR KEGG; bab:bbp_540; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_6; -.
DR OMA; HCANILI; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01920; Helicase_Rep; 1.
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; IPR005752; Helicase_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 PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..670
FT /note="ATP-dependent DNA helicase Rep"
FT /id="PRO_0000102067"
FT DOMAIN 1..277
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01920"
FT DOMAIN 278..562
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01920"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01920"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01920"
SQ SEQUENCE 670 AA; 78501 MW; A93A1AA1A3869720 CRC64;
MLFNEHQKKA ISYISGPCLI LAGAGSGKTR VIINKIVHLI KICHFDPKCI TAITFTNKAA
CEMKSRILNV LSVNVSNLVK ISTFHALGLE IIKSEIELLN IKSNFTIFDE QDQISILQEI
VSKEDRSFVR QIRQSISNWK NKLLCPNQVN KISNSSIEFK FFRYYELYNA YLKSSNILDF
DDLIFLPTIL LRDNKLSRER WNDKIKYLLV DEYQDTNFIQ YKLIKLLSSK RSNFTLVGDD
DQSIYSWRGA NIHNFESLKH DYPNLRTIIM QHNYRSSGRI LKVANALISN NLHFFNKKLF
SNLDYGSIVE IISAKNEEDE ARVILQTLML HKSNYNAQYK DYAILYRSNY QVKIFEKFLI
KFKIPYKILA NISFFSRPEI KDLIAYLRLI INPDDNAAFL RVVNRPLRGI GAVTLQKLKE
WSKKRNQSFF MASLDIGLES ILPVHNLKSL QEFVYLIQTI SYQIQLNPIE VLEKLVATIK
YEKWLMRSLK FSKLYVASIK NISIVLNWII NELKYKIMNS KKFVMKYLID IISEFILQNS
LNEDIVINND YVQLMTLHAS KGLEFLYVFI VGVEEGVLPY YRNTTMENNI DEERRLAYVG
ITRAQKKLFL SYAIQRCQYG VVINTKPSRF LRELPQSDIL WQKSKILNLN EKNNFLFKAY
KKSLKKKLLR