UVRD_MYCCT
ID UVRD_MYCCT Reviewed; 722 AA.
AC P45612; Q2SRD6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable DNA helicase II homolog;
DE EC=3.6.4.12;
GN Name=uvrD; Synonyms=pcrA; OrderedLocusNames=MCAP_0717;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 541-722.
RX PubMed=8253782; DOI=10.1016/s0021-9258(19)74345-2;
RA Zhu P.-P., Reizer J., Reizer A., Peterkofsky A.;
RT "Unique monocistronic operon (ptsH) in Mycoplasma capricolum encoding the
RT phosphocarrier protein, HPr, of the phosphoenolpyruvate:sugar
RT phosphotransferase system. Cloning, sequencing, and characterization of
RT ptsH.";
RL J. Biol. Chem. 268:26531-26540(1993).
CC -!- FUNCTION: Has both ATPase and helicase activities. Unwinds DNA duplexes
CC with 3' to 5' polarity with respect to the bound strand and initiates
CC unwinding most effectively when a single-stranded region is present.
CC Involved in the post-incision events of nucleotide excision repair and
CC methyl-directed mismatch repair (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000123; ABC01643.1; -; Genomic_DNA.
DR EMBL; L22432; AAA16212.1; -; Unassigned_DNA.
DR PIR; D49683; D49683.
DR RefSeq; WP_011387561.1; NC_007633.1.
DR AlphaFoldDB; P45612; -.
DR SMR; P45612; -.
DR EnsemblBacteria; ABC01643; ABC01643; MCAP_0717.
DR GeneID; 23778329; -.
DR KEGG; mcp:MCAP_0717; -.
DR HOGENOM; CLU_004585_5_2_14; -.
DR OMA; YQDTNRT; -.
DR OrthoDB; 137860at2; -.
DR PhylomeDB; P45612; -.
DR Proteomes; UP000001928; Chromosome.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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 PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding.
FT CHAIN 1..722
FT /note="Probable DNA helicase II homolog"
FT /id="PRO_0000102075"
FT DOMAIN 8..291
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 292..565
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT BINDING 32..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 722 AA; 83641 MW; 64492D9FF891D2E5 CRC64;
MSVDNLLDLL NDQQLAAVLN IDKPVRIIAG AGSGKTRVIT TKIAYLIEKQ NIDPSRILAV
TFTNKAAKEM KERVLQITNN SFKSPFISTF HSWCSKVLRI DGKHIGLEDK FLIIDSDDQK
RIIKSALKES NIELSENDKK TFDKKILYKI KEWKEELVDP SEAILNATST LEKNFAVIYR
LYQNTLLKNN SLDFDDLQIY VYRLFKQNNE ILNKWRNAYD YVLVDEFQDT NELQFSLIKF
LTINTNHLTV VGDPDQTIYS WRGAKLDIIL NFNKTYSNAI SIVLNQNYRS TKQILDISNS
FIKNNKFREH KEIFTNNKSG KKVVLKECNS KTSEASYVSS KIKELVKQGY HYKDIFILYR
MNAWSQEFEK ELANKKIPFQ LIGGIKFRER KVIKDAMAFL KMISIKDNLS SQRVLGLIPK
IGNITIEKII NTANLNHLNI FDLITNEDKT LLHSITKNLD ELIEVFKTAH QLYLDNTNIE
EILKYLLIQS GYENKLKIRK EQDDLENINA LYDQLKRFDE DFDPKYYSEE NKLIAFLQEE
ALTSDIDEAE QIDKVSLLTV HAAKGLENKV VFITGLNQGI FPSRISETSI NELEEERRAL
YVALTRAKDE LFLTYVKGDY SHIMQSELKP SKFIHELDKD LYEFETQFLN TLLYDSNDYK
QSSFYVSPKQ HNLYNVGDHV EHKLFGKGVV VKIINDQLQI SFTNSSYGIM MIATNNSALS
KV