ID   F9ZQ70_ACICS            Unreviewed;      1185 AA.
AC   F9ZQ70;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAY-2015, entry version 28.
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   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; Proteobacteria; Gammaproteobacteria; 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
RT   central 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
CC       highly rapid and processive ATP-dependent bidirectional helicase
CC       activity. Degrades ssDNA until it encounters a chi (crossover
CC       hotspot instigator) sequence from the 3' direction. Cuts DNA near
CC       or within the chi site, which attenuates 3'- but not 5'-
CC       exonuclease activity. The altered holoenzyme produces a long 3'-
CC       ssDNA overhang and facilitates RecA-binding to the ssDNA for
CC       homologous DNA recombination and repair. Holoenzyme degrades
CC       foreign DNA, contributing to antiviral protection. This subunit
CC       has DNA-dependent ATPase activity, exo- and endonuclease activity,
CC       3'-5' helicase activity and loads RecA onto ssDNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of
CC       ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC       phosphooligonucleotides. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01485};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01485};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits
CC       contribute to DNA-binding. Interacts with RecA.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The C-terminal domain has nuclease activity and interacts
CC       with RecD. It interacts with RecA, facilitating its loading onto
CC       ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent
CC       ATPase and has ATP-dependent 3'-5' helicase function. This domain
CC       interacts with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- SIMILARITY: Contains uvrD-like helicase ATP-binding domain.
CC       {ECO:0000256|SAAS:SAAS00048467}.
CC   -!- SIMILARITY: Contains uvrD-like helicase C-terminal domain.
CC       {ECO:0000256|SAAS:SAAS00048480}.
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DR   EMBL; CP002573; AEK56907.1; -; Genomic_DNA.
DR   RefSeq; WP_014002203.1; NC_015850.1.
DR   RefSeq; YP_004747607.1; NC_015850.1.
DR   EnsemblBacteria; AEK56907; AEK56907; Atc_0256.
DR   KEGG; acu:Atc_0256; -.
DR   KO; K03582; -.
DR   BioCyc; ACAL990288:GJBS-258-MONOMER; -.
DR   Proteomes; UP000006135; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 5.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01485; RecB; 1.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004586; RecB.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF00580; UvrD-helicase; 2.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 5.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR00609; recB; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|HAMAP-Rule:MF_01485};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00146071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006135};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00048487};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00048304};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00048455};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_01485};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00048355};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00146013};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00146062};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01485};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01485};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00048484};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00145996};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006135}.
FT   DOMAIN      469    769       UvrD-like helicase C-terminal.
FT                                {ECO:0000256|HAMAP-Rule:MF_01485}.
FT   NP_BIND      20     27       ATP. {ECO:0000256|HAMAP-Rule:MF_01485}.
FT   REGION        1    873       DNA-binding and helicase activity,
FT                                interacts with RecC. {ECO:0000256|HAMAP-
FT                                Rule:MF_01485}.
FT   REGION      917   1185       Nuclease activity, interacts with RecD
FT                                and RecA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01485}.
FT   METAL       968    968       Magnesium; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01485}.
FT   METAL      1078   1078       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01485}.
FT   METAL      1091   1091       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                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
//