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Database: UniProt
Entry: F9ZQ70_ACICS
LinkDB: F9ZQ70_ACICS
Original site: F9ZQ70_ACICS 
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
//
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