ID   F9ZQ70_ACICS            Unreviewed;      1185 AA.
AC   F9ZQ70;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   10-MAY-2017, entry version 46.
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; Proteobacteria; 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
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. Unwinds dsDNA until it encounters a Chi (crossover
CC       hotspot instigator) sequence from the 3' direction. Cuts ssDNA a
CC       few nucleotides 3' to the Chi site. The properties and activities
CC       of the enzyme are changed at Chi. The Chi-altered holoenzyme
CC       produces a long 3'-ssDNA overhang and facilitates RecA-binding to
CC       the ssDNA for homologous DNA recombination and repair. Holoenzyme
CC       degrades any linearized DNA that is unable to undergo homologous
CC       recombination. In the holoenzyme this subunit contributes ATPase,
CC       3'-5' helicase, exonuclease 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, ECO:0000256|SAAS:SAAS00597767}.
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DR   EMBL; CP002573; AEK56907.1; -; Genomic_DNA.
DR   RefSeq; WP_014002203.1; NC_015850.1.
DR   RefSeq; WP_014002203.1; NC_015850.1.
DR   RefSeq; WP_014002203.1; NC_015850.1.
DR   EnsemblBacteria; AEK56907; AEK56907; Atc_0256.
DR   KEGG; acu:Atc_0256; -.
DR   KO; K03582; -.
DR   OMA; IMIGDPK; -.
DR   OrthoDB; POG091H02P3; -.
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:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP.
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   InterPro; IPR034739; UvrD/AddA_N.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF29; PTHR11070:SF29; 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   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00753523};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006135};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00753507};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00753512};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00627189};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00753531};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00493105};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00753525};
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:SAAS00753541};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00753533};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006135}.
FT   DOMAIN        1    468       UvrD-like helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51198}.
FT   DOMAIN      469    769       UvrD-like helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51217}.
FT   REGION        1    886       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   ACT_SITE   1091   1091       For nuclease activity.
FT                                {ECO:0000256|HAMAP-Rule: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
//