ID U4T3L0_9GAMM Unreviewed; 1490 AA.
AC U4T3L0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=M917_2799 {ECO:0000313|EMBL:ERL54651.1};
OS Psychrobacter aquaticus CMS 56.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1354303 {ECO:0000313|EMBL:ERL54651.1, ECO:0000313|Proteomes:UP000016761};
RN [1] {ECO:0000313|EMBL:ERL54651.1, ECO:0000313|Proteomes:UP000016761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMS 56 {ECO:0000313|EMBL:ERL54651.1,
RC ECO:0000313|Proteomes:UP000016761};
RX PubMed=24201199;
RA Reddy G.S., Ara S., Singh A., Kumar Pinnaka A., Shivaji S.;
RT "Draft Genome Sequence of Psychrobacter aquaticus Strain CMS 56T, Isolated
RT from a Cyanobacterial Mat Sample Collected from Water Bodies in the McMurdo
RT Dry Valley Region of Antarctica.";
RL Genome Announc. 1:e00918-13(2013).
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:ERL54651.1}.
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DR EMBL; AUSW01000035; ERL54651.1; -; Genomic_DNA.
DR RefSeq; WP_021815410.1; NZ_AUSW01000035.1.
DR STRING; 1354303.M917_2799; -.
DR PATRIC; fig|1354303.4.peg.2757; -.
DR eggNOG; COG1074; Bacteria.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000016761; 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; 4.
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: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}.
FT DOMAIN 32..610
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 651..940
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..1086
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 1130..1490
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 1370
FT /note="For nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 1211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1370
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1490 AA; 169075 MW; 4BEB27137B733704 CRC64;
MTDFSDTTDI STQPHLFDEY SSECDDLTAM AEPKADVTPA VAVELTGKHL IEASAGTGKT
WTLTGIVLRL LIEARRAPEQ IIATTFTRAA AAEMRQRIHD RLVEFYQLLQ WINNLSANTN
NKNSLYPNIL QVMPDSNEDR PAGNDLSIDS NAQTDIDAFN QDLDHDQQAA KEKRAQVRKA
RDEWLIQQAK HVRLDKIMQD PVNLHLVGYL LDHVYSYPMA EALRRTALVL TTLDKLFVGT
LDSLAQKWLT EYSSETGHQQ GMAIIEDSSI EQVTDSIIHD ELRQFQSRLY HEQPKLYALM
DQQGNLTAVS DHKKFVSRSL NFISAPIDEI RLEEGFDFTA YEKLIAEFAQ LDLADIQPYL
NPDYRKSQGF NGRSNLTKQF DALVEVHQKI AKYQLAFNSY LNESERKILT SLQDARYPDE
DGKIKNFNKN KEKEHQTLFE LETISKLMTL LDMVEGLNQH IVLILANLNR HIVLAVRDRL
PVILEERGET TFSLQMVRLN QALTGRQGHK LARYIRHHYP VALIDESQDI NGEQAIMIES
IYLPKNKQTQ EEKDKPSGSS KTNREFLLLV GDPKQAIYGF RGGDVSNYNY MKAQFDTSSR
WTLDTNRRSN AGVIHALNCW FGMPTATTDN NKLSQLGSGI YYQYIKAEKL EYELSWFKYL
DIQGNNLVTE VLSAQPVSVL HLPSGKDVEL EYDEHEITAR HIATLLSSGQ TLKGKAIQPS
DIGVLARAKK DLKRVEDELV KLGVPTLTTS DVSILETIMA EDIAALLSAM LYPYRHDMIN
RVLTSHLYGL SIKDVKAMMT DHESGIIEAS STTRAHSKNA STIDNNKSYQ DFITYLKEGA
QRWQHFGILS ALHYLLDKSP LQPQGVWQSL AAHTEGDRHI MDLRHLMDVL AQYGTGMGEH
ELLAWFRQHI DAAPNSDWAK QYPLPTESGV QLMTIHKSKG LEFPIVYVLG MGNASRKSGN
KENYGLYLYN AAQAPSAMVQ QSLQNQLTGN KRRFSPLQGS ATTDDYYTDI ETNEGFDELR
RLGYVAFTRA SEQLYVVLQD PKKNVNPGLK PVFYWFDSVE ATFELPDRLK GTIGMIRGHK
VNEFYNDNYA NHAKSAGLND ATPLTTIKPM TETIEYDAFS EVMKTNYFYG WAKTSFTALA
RQLDESTQAM VIVDERIDDA IDIDMRNTSA SDEPLSNSSE SPKDVNELTL KLEDDIRFTF
VKGANAGTFL HEIFEKIDFT NKSQWSGVID RAVNSYQLPL VYSSAEQQSR RLQSNKDIAG
VLLDLDSIDT TKHDALINWI EEVIDAPLLA SNQPLRSLSA SQRFAELEFN MGLSERFKAQ
DINKLFQQYL PNDIDKHVNL VAQNKTHLYR YLRGEIDLVY EHAGRYYVVD YKSNFLGNSL
SDYDESTLKQ AMSKAGYWLQ AAIYQVALHR FLSMRIQDYA GNEDKYLGPV EYVFLRGVYD
PCSQAINNTS SNTREPDGST AHNNRYGLVT WDIPIDFIKG LDTLFGLPDS
//
