ID A0A1Q8IZ69_9BURK Unreviewed; 1146 AA.
AC A0A1Q8IZ69;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RecBCD enzyme subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01486};
DE AltName: Full=Exonuclease V subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE Short=ExoV subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
GN Name=recC {ECO:0000256|HAMAP-Rule:MF_01486};
GN ORFNames=BTH42_08620 {ECO:0000313|EMBL:OLL32007.1};
OS Burkholderia sp. SRS-W-2-2016.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1926878 {ECO:0000313|EMBL:OLL32007.1, ECO:0000313|Proteomes:UP000186182};
RN [1] {ECO:0000313|Proteomes:UP000186182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS-W-2-2016 {ECO:0000313|Proteomes:UP000186182};
RA Chauhan A.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC rapid and processive ATP-dependent bidirectional helicase activity.
CC Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC Chi site. The properties and activities of the enzyme are changed at
CC Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC and repair. Holoenzyme degrades any linearized DNA that is unable to
CC undergo homologous recombination. In the holoenzyme this subunit
CC recognizes the wild-type Chi sequence, and when added to isolated RecB
CC increases its ATP-dependent helicase processivity. {ECO:0000256|HAMAP-
CC Rule:MF_01486}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01486};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC -!- SIMILARITY: Belongs to the RecC family. {ECO:0000256|HAMAP-
CC Rule:MF_01486}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLL32007.1}.
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DR EMBL; MSDV01000020; OLL32007.1; -; Genomic_DNA.
DR RefSeq; WP_075297914.1; NZ_MSDV01000020.1.
DR AlphaFoldDB; A0A1Q8IZ69; -.
DR STRING; 1926878.BTH42_08620; -.
DR OrthoDB; 9762834at2; -.
DR Proteomes; UP000186182; Unassembled WGS sequence.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.10930; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01486; RecC; 1.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006697; RecC.
DR InterPro; IPR041500; RecC_C.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR NCBIfam; TIGR01450; recC; 1.
DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR Pfam; PF04257; Exonuc_V_gamma; 1.
DR Pfam; PF17946; RecC_C; 1.
DR PIRSF; PIRSF000980; RecC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01486};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Helicase {ECO:0000256|HAMAP-Rule:MF_01486};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01486};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01486}; Reference proteome {ECO:0000313|Proteomes:UP000186182}.
FT DOMAIN 824..1086
FT /note="RecC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17946"
SQ SEQUENCE 1146 AA; 125632 MW; 0844EFCB334690CB CRC64;
MLQLFYSNRY ETLVGALLDD LGEAPSDPWT ARPVIVPSAA VRRRLELDIA ARQGICANID
FGYLAQWLWA RIGGVIDVPK HSPFAPDRLV WRCYRLLADA DEALPWNASP RLRTYLDAAD
PSMRYELARR VATVLDHYLT YRPEWLLQWQ KGGSIFASGT PDDTGPRLTG ASESAREDER
WQAALWRAVL AELAQSAEEA SGAARGSVNA LPPAYRFLDE IGKLDLDAIS KAQWPEAVSV
FALPTMPPLH VALLRALSRW IDVRLYVMNP CREFWFDVVS EGRVQALDAA GKLDYQEVGH
PLLAEWGRQT QAQLHMLHEL TESAASAETG EFSENPEPSW LAAVQNGILE LRAESDAEEL
PIERGIEVHV CHSLSRQLEV LHDRLLGWFD EFDDLQPSDV LVAVSDLAAA GPLIDAVFGT
TPAGDTRRIP YRITGLPPSQ ANPVARLLLD WLALPERSVG APDLIEWLRV DAIAVRYGID
ANALEAAQEW LAAAGARRGL APLEPVGEHV PVARHTFADA LTRLYLGYAM PAGGEPVDAW
LPVEGADGSG AELLGRLSRF VEDVESFAAN CALERTPAEW SQLLLETLGQ CFDGGVEFAD
SLAAVRDALD AMSAAMQAGA QQVPLPASVV RSALSEALDD PARGGVPWGS VTFSSLTSLR
GLPFRVVCLV GMDDGVLPSL ARADEFDLMA AFGKAGDRQR RDDERNLFLE LLLAARERLF
ISYTGRSIRD NAPLPPAALV DELLDHLAQV SAGEHASPAE VEHARREFLV EHPLQAFASD
YFAAQPDLFT YDADRAELAT LLAEPQHAPA APFFDQPLPP EDTREIEFDD FVRFWRHPAR
ALLRDRLGIA LADAQGELLD TEPFELDYAG RDALADRLLP VLLDTDTDDD TMFGRVQRVA
AASPELPNGA TGAVWRSREL NALRQLALAV RREVASGVER LPFALEIKPR WPSFDDSAAH
GQGPIRLFGA YDAPLREAAE ATAATAATQP PLQLRGTLNL LTGTGQVIFR YAKATARDYL
SAWLAHLVYC AAQPQGPRRT VWHGSGESFE FAPVAAPLEQ LAPLVALYRA GRRLPLRFFP
KSAWTKVSES DSAAQGVWIN DRVRGESDDP ALRIALRGTP LTLDEPFGSL AALVYKPLLQ
HLRSVS
//
