ID A0A2X0WEV3_9GAMM Unreviewed; 1359 AA.
AC A0A2X0WEV3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:SPT68907.1};
GN ORFNames=NCTC13093_00257 {ECO:0000313|EMBL:SPT68907.1};
OS Anaerobiospirillum thomasii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Succinivibrionaceae; Anaerobiospirillum.
OX NCBI_TaxID=179995 {ECO:0000313|EMBL:SPT68907.1, ECO:0000313|Proteomes:UP000250086};
RN [1] {ECO:0000313|EMBL:SPT68907.1, ECO:0000313|Proteomes:UP000250086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13093 {ECO:0000313|EMBL:SPT68907.1,
RC ECO:0000313|Proteomes:UP000250086};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; UAPV01000001; SPT68907.1; -; Genomic_DNA.
DR Proteomes; UP000250086; 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; 3.
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; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 2.
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:UP000250086}.
FT DOMAIN 1..544
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 570..854
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..1012
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 1020..1359
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 1262
FT /note="For nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 1098
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1359 AA; 155935 MW; D33509893DA728EF CRC64;
MSSNTLVIKN FDLKLSSLIE ASAGTGKTYT ISYLVIRLLL GSGMHNNTAH KDGPLNLENI
LIVTFTEKAT ADLKARVREK IRYARLGFEK YLKDREHFDK TQYETQLVEI IEEFEDDNLK
TLSGALQILK RAERSVDTAS IYTIHSFCNK ALNRIYAFET GEAFENEFVI DIGKYQKEAA
QGMWRYLFYP ESDRLKLIED NYLESTDGYT LFNKYNSYLE KVVLPDKKQG FLGYNIINLP
LKLKATSAVE ALDELVAYVK IHDSLTILGD IFKRRLCDQD SVNCIKNRLY ALYNPKSGNS
NGFAFKSSDK SLLSQKRGLL FLKLVNQAID DIDNLDLTQV QEAVDAIVGN DFDEPYKYFV
DGSRIRSLTS ASVADSNLLA ESCKYFYEFA LECSELLNEF TDIVLLINLV TVICIRERVE
LLCKRDKVIY SNDVLTRLFY ILNTKESGDA LARLLRQRYR VAMIDEFQDT DPIQFNIFKK
LYLNEEAQDN GAACYLIGDP KQSIYEFRGS DINSYLKARN LIEKLQQRAG GVGILTLDTN
YRSDRTIIES VNAMFSSDIG KSDKNAFISD NIKYLKVGHV TKDSYLKDTD SLSLAQNGTT
VSIIDTINKY KAAELRLMVA RRAALDIVHL LSHGRIVKDG VECEIRPGDI AVLVSSGSEN
EYIAEELEKL NIPSVYYSDR QSVLKDASGE KPSEDAKNII YLMQAMMEPT RRSTLNRLLG
SRLLGLNGKE FDALRSDEHY EHEIELLNKC RLVWERDGFL SAFATWYLDS SHDCLRRRLS
EHGGLRRISN LYQIAELIQG VHNSISGVMA QLRYFIDLIE SQDSTLIADD STFEKRLDTQ
RDQVKVLTIH KSKGLEFPIV IMPFLWFKAQ KKEMADQRVI PYYDENEGAY VIGFNATASK
NSRDLASGCE NRRLLYVAVT RARYANYMYA VDTQHVRGYE QSPVNALLSG RSERKGSFEI
TNDNLHAFSS VSDSMHLHEL TVKDGQVLHT GEREYTYRRE IHDYDEFELG IFFPESIDRR
FVFTSYSAIT KNAMLAESYR AALLKNDENY VADEFTDEMA DKDVSVILPS LAHSGLDVQQ
CFNNLNYPKG AVFGTIMHNI FEKTAFDRLD GGALAQAVAD IVLKEGDSNA IKLKKSWLYG
CPDEDYRFYA HNSLMAISTW FDRAIRQDLL CRTDKSYALC DLKEMDYIAE MQFLMPCSAF
DIEDFNRLCQ KEALRVFKDC PDKSFIEGMA LQKQIIDGYL NGSLDLVLRF KIDNEYKYFV
LDYKSNYLGS SLSDYRAQNI GRVMFNEHHR YDVQYLIYTV VLHRYLKLRL KDYDYDRHMG
GVLYLFVRGM GHDNEHGVFH TKVDYDLVLQ IEQLLYPKE
//
