ID   A0A4D6XS20_9GAMM        Unreviewed;      1162 AA.
AC   A0A4D6XS20;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-SEP-2019, entry version 2.
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   ECO:0000313|EMBL:QCI17260.1};
GN   ORFNames=D9V62_02300 {ECO:0000313|EMBL:QCI17260.1};
OS   Buchnera aphidicola (Aphis helianthi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=2315802 {ECO:0000313|EMBL:QCI17260.1};
RN   [1] {ECO:0000313|EMBL:QCI17260.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ahe {ECO:0000313|EMBL:QCI17260.1};
RA   Chong R.A.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QCI17260.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ahe {ECO:0000313|EMBL:QCI17260.1};
RA   Moran N.A.;
RT   "Genome evolution of the obligate endosymbiont Buchnera aphidicola.";
RL   Submitted (MAY-2019) 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
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:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in
CC         either 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5;
CC         Evidence={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:SAAS00709641}.
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DR   EMBL; CP034894; QCI17260.1; -; Genomic_DNA.
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; IPR038726; PDDEXK_AddAB-type.
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:SF23; PTHR11070:SF23; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
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:SAAS00146071}; Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS01099294};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS01099287};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00745286};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS01033115};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00553650};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00146062, ECO:0000313|EMBL:QCI17260.1};
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:SAAS01033141};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485,
KW   ECO:0000256|SAAS:SAAS00145996}.
FT   DOMAIN        1    440       UvrD-like helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51198}.
FT   DOMAIN      483    735       UvrD-like helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51217}.
FT   REGION        1    874       DNA-binding and helicase activity,
FT                                interacts with RecC. {ECO:0000256|HAMAP-
FT                                Rule:MF_01485}.
FT   REGION      887   1162       Nuclease activity, interacts with RecD
FT                                and RecA. {ECO:0000256|HAMAP-Rule:
FT                                MF_01485}.
FT   COILED      100    120       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE   1066   1066       For nuclease activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01485}.
FT   METAL       942    942       Magnesium; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01485}.
FT   METAL      1053   1053       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01485}.
FT   METAL      1066   1066       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01485}.
SQ   SEQUENCE   1162 AA;  139028 MW;  5F1FA975D3D63731 CRC64;
     MKKKLNIFNI PCNGIKLIEA SAGTGKTTSI VLMYLRLLLG IGSKKNNKPL LIQEILVVTF
     TNFAKEEIYK RIKKNIEQLY LYCITKNTNN SILKPFFKKI KNLEETIHLL EQAKKNINHM
     SIYTIHGFCK NILKLNFLNF HQKIIEDEKL LYLQATEDFW RSYFYEVPKK IINIILQDYK
     NPESLLSELK PIFNFRKVYF KKKFNKNQNL ITCHEENINI INIFKKKWLD YNPIILNIVK
     ELKPNKKIYN DFNISRWQKN ITKWAESETE DYQIPITLKY FLKDTIIKNI KSNQIPCHIF
     FQDIEKILKI KFSLKDIILF QAIKKITKFL NKEKQKKFLL GFNDLLDTLL KYIKKEKTLR
     KLIIEKYPIV FIDEFQDTDI QQYQIFNILY NKNNKQTGLF LIGDPKQSIY SFRGADIFSY
     LYAKSKIKKY YYLNNNWRSS KNICKAINYL FLRNKNPFLF KDIPFIKISS SFNNQNIQFK
     IKGRIQTAIS FFFKKKEKIY IKDYQEWISK QCANEICYWL ICAKKGEAIL INKDKERILK
     TNDIVILVRN KNEANIIQNS LEKVNIQSIY SSSNQNIFKT TDAFELLIIL QTILQPTNIK
     LLKQSIFTHI FYNILLQGKK QNKIKQSYFI IKKLYEYREI WKNVGIFYTI KTIVLDYQKY
     SNDLNKTQYY QKNINFLHIA ELLEKQSEYL YQDSSLIRWF ENKILEKQNI LEDEHIRYFK
     QSNAIKIITI HKSKGLEYPI VWIPFAATYK KSNVYLYHDK KTFKMFLDLN QNKETEKIAD
     EERLAEDLRF LYVAITRSIF HCSIGMGDII NKKHQKTNNN HKSALGYIIQ RGCYMNYNNL
     LNELSLLNAK SYIKVKYDTM NIKLPYTKQD VYLLSPPQYI IKKIQNCFQI TSFTKLKKEH
     VSLNKSQDNY NINNILDYKS IYKKQIIFEN FPRGEKTGIL MHYILNKINF IEKLNINFFY
     KVLKQYEFSE KWAPILMSWV NNIINVKLKN INVNLSMLKQ NQYIKEMKFF LPIQKTLNSI
     DFNHIIQSLD PISSLTSKIS FNPITGILTG SIDLVFIWNE RYYIIDYKSN YLGDNQNLYS
     LKNIKKEIIK NRYDLQYQIY TVALHQYLTK KLKKYKYKNN FGGVFYMFLR GINKINENNS
     IFYTIPDYLL IKKLINLFLI KN
//