ID F9ZQ70_ACICS Unreviewed; 1185 AA.
AC F9ZQ70;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01485};
DE AltName: Full=Exonuclease V subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE Short=ExoV subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
GN Name=recB {ECO:0000256|HAMAP-Rule:MF_01485};
GN OrderedLocusNames=Atc_0256 {ECO:0000313|EMBL:AEK56907.1};
OS Acidithiobacillus caldus (strain SM-1).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK56907.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK56907.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK56907.1,
RC ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(2011).
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 contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA
CC onto ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}.
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 Evidence={ECO:0000256|ARBA:ARBA00034618};
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_01485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01485};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01485};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. Interacts with RecA. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with
CC RecD. It interacts with RecA, facilitating its loading onto ssDNA.
CC {ECO:0000256|HAMAP-Rule:MF_01485}.
CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent ATPase
CC and has ATP-dependent 3'-5' helicase function. This domain interacts
CC with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01485}.
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DR EMBL; CP002573; AEK56907.1; -; Genomic_DNA.
DR RefSeq; WP_014002203.1; NC_015850.1.
DR AlphaFoldDB; F9ZQ70; -.
DR STRING; 990288.Atc_0256; -.
DR GeneID; 69613550; -.
DR KEGG; acu:Atc_0256; -.
DR HOGENOM; CLU_001114_6_0_6; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000006135; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd22352; RecB_C-like; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR HAMAP; MF_01485; RecB; 1.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR00609; recB; 1.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01485}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01485};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01485}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01485}; Nuclease {ECO:0000256|HAMAP-Rule:MF_01485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01485}; Reference proteome {ECO:0000313|Proteomes:UP000006135}.
FT DOMAIN 1..468
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 469..769
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..891
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 887..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1185
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 1091
FT /note="For nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 20..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 968
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1078
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1091
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1185 AA; 132829 MW; 33D61DFEBADF39E5 CRC64;
MSRVLDPLSL PLQGSALIEA SAGTGKTYTI ATLYLRLLLG HGEPATLPRQ PREILVMTFT
RAATEELRER IALRLYAAMT ALREGAPPAS GDALLQRLLR DYPDPATRAA AIIRLENAFN
SVDEASIHTI DAWCHRVLRE HALATGHDPD AEILTDSAPL RIRAVQDFWR REIYPLQRAA
PWWLQRTPDP ETLLEQVAGL PWLDPPLPAP RAAFHDWLEN AAAPLLKAGT ELKAQWSSTL
RDTYGRWLRE LADRDPYPLN RKSLPPEKLQ GALQSLDQWC VEKEAAVPTA MATVAKLGSA
LAECVKKGMH CPAPPSQAQF DTFLAALQQW QVDDEVLHGQ ALAQAAASMA ALYGEEKQRL
RQLEFNDLSR ALWNGLRGPG GEALAEALRQ RFPVILIDEF QDSSARQYAI FERIYRPSEP
WPDSLMLLIG DPKQSIYRFR GADLDSYLRA RADTAPRHYV LGTNYRSAEP LVGALNALYA
RADERCPGGA FDYRGEGDDP LPYQAVAAAG RSQRWQLGGQ EGPAITFAQH PLALTKEEFL
THFAEWTAAT IAQLLGDSTS GFVGADGKLR RVGAGDIAIL LRDRKEAAIM LSALHRRGLP
AAFLSEKQSV YHSPEAEELR LWLFALLHPE DEAALRCALA LPLLGLTQHD LWRLDTDEGL
WAQEVERLRE YARIWAHSGI LTTLHRRLHQ QATAARILAR PDGERRLGNL LHLGELLQRA
SQHLEGREAL LEHLQREQDS EDNPADSHVL RLESDAHCIR IRTIHSAKGL QYPLVFLPFI
AATRKDGNIP PWQVVTGDDQ STLSWQSPSA ELMDRERLRE DLRLLYVALT RAEYALWLGL
AAGKTASTPL WWRSAVGRLL GADEGKTPDQ CLETWKRHPA CRVLAADTIP SAPAPRSAEP
SEPRRTPPVY TARFERDWSI HSFSRLSQSL QTSVGPYPSP DRVDPGAQAA GQGWHTFPQG
PGAGRFLHEL LQWLWRDGRW PEDWREDFLH RCDERGYAPW GPVLVHWFAV LRASPLGSLG
TTFAELRGAR TEMPFWFPSQ HLPTNQLDTL CRRYLLPGRE RPILGEQNLH GLFHGFMDLV
FAVDGRYYVL DYKSTRLGEN DAAYGDTAIG EDVLEHRYEL QAALYLLALH RHLRQRLGRQ
YRTEQHLGGA WLWYLRACAT AGGGLLYLAA DPQLLDALDS AVGRS
//