ID A0A315F193_9BURK Unreviewed; 1268 AA.
AC A0A315F193;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=B9Z45_02540 {ECO:0000313|EMBL:PUE62708.1};
OS Limnohabitans sp. 2KL-17.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1100704 {ECO:0000313|EMBL:PUE62708.1, ECO:0000313|Proteomes:UP000251446};
RN [1] {ECO:0000313|EMBL:PUE62708.1, ECO:0000313|Proteomes:UP000251446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2KL-17 {ECO:0000313|EMBL:PUE62708.1,
RC ECO:0000313|Proteomes:UP000251446};
RA Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA Simek K., Ghai R.;
RT "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL Submitted (APR-2017) 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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PUE62708.1}.
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DR EMBL; NESK01000004; PUE62708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A315F193; -.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000251446; Unassembled WGS sequence.
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 CDD; cd22352; RecB_C-like; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 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 NCBIfam; TIGR00609; recB; 1.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
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 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|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01485};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01485};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000251446}.
FT DOMAIN 19..500
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 525..801
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..950
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1268
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 1163
FT /note="For nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 1037
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1268 AA; 140224 MW; 88785197DCD7BE4C CRC64;
MNPQTLNPQP HSDSQSEVQV ASHPLEALSF PLWGSRLIEA SAGTGKTWTI AALYVRLVLG
HGEQCEKDEE GEQGLRPLMP HDILVMTFTR AATRELSDRI RARLTEAAQV FRSPDLLDAK
DTFLKGLLSD YPDKSSREKA AYRLALAAQA MDDAAVYTID AWCQRMLREH AFDSGNLFEE
SLVADEAALR LEAVQDYWRE QLYPMNAPSV TEVLGIWRDV AALEQDMRQL LNVEALPEAL
PGQSLGDALA RAAEEKAQAL AQLKRGWPEQ ADALLDWLGD VPAVENSGWK KRSLSLTNCS
KWLGSLKLWA QGEGGYDELK KAMGKTGWER FTPEGMAACR EDDKPYTLPP QCQAFADLQS
ALQSLPQARV AARIHARTRV AERLAWLKQR TAQFGFADML QRLDAALQRG DDGKRLALRL
RQQFPVALID EFQDTSPLQF RIFDHIYCTA ENLRETALLL IGDPKQSIYG FRGADILSYL
TARVATAGRH YVLDTNYRST QAVVNVVNRW FEVGDARSVQ GAFGYARPDG SNPLPFQPVK
ANSRAEVLCH QAGEVPAMTL AHAPELASHR DAMTHMSALC AEQIVAWLGD ASTRFVQDGQ
ADQRLKPKDI AVLVRTGKEA DAVRHALSVR GVASVYLSDR DSVFDSDEAG DLCLWLRAVA
EPQDMRRLRA ALATRTVGLT LPELHHMAQH GDALDAYADQ MHALRQTWQT QGVLAMVRRS
LHALNLAARW RGQAQGERRL TNVLHLAELL QSASMRLDGE QALIRWLVQQ MDENAESDEQ
TVRLESDEDL VKVVTIHASK GLEYPVVCLP FAHSHRVVRA DKTTVLSLTD AQGERHNQLQ
FTAQDVQSAD ADRLREDLRL WYVALTRARH ALWVGWAAVH KPRGKDCQNH LSAAGRLVGG
DSQHEAHAWP ELLQALLTDA HGQPLPVQLQ TADSAVGLSR WQRDDDLPVL REVQACTAVI
DKRWTIASFS RLARDLSSQP VLQAVLQMAT PRPADDEPPD EGMGLAIPSG AAAPRATAAV
SPWHGFARGP SAGNFLHDQL EWLAADGFAL QPGTPTAERL LKRCDRAGYK AQADVVVNWL
SRVVAQPLRG PDAQLNALVT VLPEMEFWLP ADRLHAQEID ALCRQHLLVG VPRPKLPEAQ
LHGMLMGFAD LVFEHGGRYW VLDYKSNHLG ADDAAYTAEA LDQAMAHHRY EVQAALYMLA
LHRLLRARLG AAYDPAQHLG GAVYLFMRGI DGSAGGCCTL PAPLALMDGL DAMLGRPTDA
ATQPRKRA
//
