ID   A0A4D6XS20_9GAMM        Unreviewed;      1162 AA.
AC   A0A4D6XS20;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   14-DEC-2022, entry version 12.
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, ECO:0000313|Proteomes:UP000298759};
RN   [1] {ECO:0000313|EMBL:QCI17260.1, ECO:0000313|Proteomes:UP000298759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ahe {ECO:0000313|EMBL:QCI17260.1,
RC   ECO:0000313|Proteomes:UP000298759};
RA   Chong R.A.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QCI17260.1, ECO:0000313|Proteomes:UP000298759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ahe {ECO:0000313|EMBL:QCI17260.1,
RC   ECO:0000313|Proteomes:UP000298759};
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 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=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
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; CP034894; QCI17260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4D6XS20; -.
DR   Proteomes; UP000298759; 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   Gene3D; 3.40.50.300; -; 2.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR004586; RecB.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 2.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 2.
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   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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01485};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_01485};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_01485};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01485};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   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}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01485};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01485};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01485};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01485}.
FT   DOMAIN          1..440
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          483..735
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          1..874
FT                   /note="DNA-binding and helicase activity, interacts with
FT                   RecC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   REGION          887..1162
FT                   /note="Nuclease activity, interacts with RecD and RecA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   ACT_SITE        1066
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         942
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   BINDING         1053
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   BINDING         1066
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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
//