RECB_HAEIN
ID RECB_HAEIN Reviewed; 1211 AA.
AC P45157;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Exonuclease V subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE Short=ExoV subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
GN Name=recB {ECO:0000255|HAMAP-Rule:MF_01485}; OrderedLocusNames=HI_1321;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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:0000255|HAMAP-Rule:MF_01485}.
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:0000255|HAMAP-
CC Rule:MF_01485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01485};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. Interacts with RecA. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01485}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01485}.
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DR EMBL; L42023; AAC22966.1; -; Genomic_DNA.
DR PIR; D64116; D64116.
DR RefSeq; NP_439472.1; NC_000907.1.
DR RefSeq; WP_005694451.1; NC_000907.1.
DR AlphaFoldDB; P45157; -.
DR SMR; P45157; -.
DR STRING; 71421.HI_1321; -.
DR EnsemblBacteria; AAC22966; AAC22966; HI_1321.
DR KEGG; hin:HI_1321; -.
DR PATRIC; fig|71421.8.peg.1373; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_0_6; -.
DR OMA; KQSIYRW; -.
DR PhylomeDB; P45157; -.
DR BioCyc; HINF71421:G1GJ1-1346-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; 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 GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 4.
DR PANTHER; PTHR11070:SF23; PTHR11070:SF23; 4.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
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; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1211
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102047"
FT DOMAIN 1..485
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 500..772
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 1..916
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 927..1211
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT ACT_SITE 1120
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 997
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1211 AA; 139858 MW; 37B76430651FAD68 CRC64;
MAETIPLNPI TLPLNQISLI EASAGTGKTY TIGSLYLRLL LKAGENNFSR PLNVEEILVV
TFTEMATEEL KKKIRERITD AINKLTAFAK TQDKSAFKND EFLTALCDNL NIFEAIHRLK
LAEQNMDLAA IYTIHGFCRR MLMQYAFHSG IHFNLELIKD QSDLLVRFAN EFWREHFYPL
DFESANFIAT ELVSPANVLS LLKADLGKDL QVEIENKQAL SVPIQIFLPQ YLGGYQKALN
ELKAFWLESA DEISAIITNE LVKDYPKDQL KSLNRKKYQV KRLGDWINKI NQWSNNPRDY
QINTTLKDYF LQSSIEKNCE ESTDKNKDKK PATPFYSPIF ADLEKRVNAL MTPDLLSKLT
LYHYRQGLQQ KLLDYKLNHQ EKSFDDLLRL LCEALQDAQG DELAEMIRFQ YPFAMIDEFQ
DTDSQQYAIF SKIYRDNPEK NTGFIMIGDP KQAIYRFRGA DIFTYLKASD EAQSRFELTK
NYRSEKHLVD GVNALFDFPQ SPFIYQNIKF TAVDSRDDHL RFYLNGKVEP AYRFYLTESD
KVNKTEMAKI CAISIQHWLK SAAENQAVFQ NEDTYKTLQA ANIAVLVRDK NEAALVKNEL
QKLGIASVYL SDQNSVFDSN VAKELAWVLK ACLNVAERPI LNAIATALFG LNAADIHQIQ
QNEADWQRWA DSFAQYQQTW QRQGILAMLH QILLEQGISE RLLSQATGER DLTDFLHLAE
ILQQAATLHE SEAALLSWFE KQIQGEARQE AQIRLESERQ LVKIVTIHKS KGLEYDLVWL
PFLAAPSKDP SKKYINIYYS KERDETLWDI ENRNLNALCE ETFAEELRLL YVALTRAKYQ
MAFALPAQFD KKWNALHYVL SQGEIGKEIN LSDSKDTETL LQTFKEKMQD NVEICTKPNL
EALPTLSINT KNDDFKASEF TGNIEQDWRI TSFTSIEQAH RRQNYFTESA GKKHAVFDDA
KDYDSQNAIE ISTALLNENE SNILDLPRGK QVGTALHRHF ENCYFSDLAN TEEIDKLRQS
LQLDETFTES LQNWLQQISH TPLSNEIGIA LADLANKDCI KEMPFYLAIR EHFDVEAFNH
TLKAHHHLPS ESLQFEQIQG MVRGSIDLVF RHNGKYYLVD YKSNFLGSTL ADYNQEALKK
EMLHSHYDWQ YLIYTLALHR YLQSVVPHYD YARDFGGVFY LFLRGMNGEP QSGVFYDRPS
VELITELDGV F
