ID R8Y383_ACICA Unreviewed; 1232 AA.
AC R8Y383;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=F935_02724 {ECO:0000313|EMBL:EOQ61952.1};
OS Acinetobacter calcoaceticus ANC 3811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=1217690 {ECO:0000313|EMBL:EOQ61952.1, ECO:0000313|Proteomes:UP000014041};
RN [1] {ECO:0000313|EMBL:EOQ61952.1, ECO:0000313|Proteomes:UP000014041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3811 {ECO:0000313|EMBL:EOQ61952.1,
RC ECO:0000313|Proteomes:UP000014041};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. ANC 3811.";
RL Submitted (FEB-2013) 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:EOQ61952.1}.
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DR EMBL; APQJ01000011; EOQ61952.1; -; Genomic_DNA.
DR RefSeq; WP_016139416.1; NZ_KB976986.1.
DR AlphaFoldDB; R8Y383; -.
DR PATRIC; fig|1217690.3.peg.2702; -.
DR HOGENOM; CLU_001114_6_1_6; -.
DR Proteomes; UP000014041; 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 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; 2.
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}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01485};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01485}; Exonuclease {ECO:0000256|HAMAP-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};
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}; Nuclease {ECO:0000256|HAMAP-Rule:MF_01485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01485}.
FT DOMAIN 4..488
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 504..774
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..900
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 922..1232
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 1132
FT /note="For nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 990
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1232 AA; 142732 MW; 766AB99B5E1B90A2 CRC64;
MNSRVQVSYQ PIIDIEFSGL HLIEASAGTG KTYTLSSLMV RIFLEKYLPR QVIATTFTRA
AAAELKSRIR ARLVETYRYL ETKRSFTEHE LMMQAEQEPD LLLQHILKSF ATRIAYACER
LKLIIDQLDE LFVGTLDSFS QKLLREFAFE SGKIERAQIT DDAKTYSRQL IHDVLREWIQ
SQPQTVIDAL YLAGELKSVD GFVKLVEDSL NFSSAHFKLP EKPIIQFEQL AQLKQLATEI
DLSLLEPYYQ LDGEHYKHVS GTIFRNGAFN KLFSECLPQL LQVLTQSDSI LVFDGSLTAQ
RELVFKFLGQ LADQKVFKKC PAEISDGFYQ HPCIQQIQHL FGVLKNYAEQ FDQLHIFLKA
YLCVEVKKRL PQVLQNKGET TFSQQIRTLS EALKGEQGQR FAVFVQARYP LILVDEFQDT
NQDQDDMLAS IWRHPERYQK GCMIMVGDRK QAIYGFRGGD MLTFLNAYKD IQTKHGREYK
LIHNHRSVAD LVEVVDALFQ RQMDFGEEVQ YDPIRAGTRP HPVLIEQNNH NPHPLRWLML
KDKETEAQQV AWKIRDLLNQ SHAGQLYFQK DAQTQTLNED DIAVLSRNHD GLDKVQFELE
RLGIRVNRPS KRSVFDCTIA QDVGALLTAI LHPYDEAKVK RALISRLFAM DLKQLLQLEQ
TAEGLSQFMT GFDTIRELWS AQGFLVAWQQ CLIQFDIWQN LVAAQSKDNE RVVVNLRHLT
EILSQHSEKY SGAQNLYHWY LKQLGSPLDR DWELERKLSS EAGVQLMTIH QSKGLEFKIV
FLLGADKPFR ENNKTLNFST QDVVQPDSSQ TLTQRVVAIA DKTYLNEVEL KQHEERALAE
QNRLWYVALT RASHRVYALL QDIDGKSVSG LAFWKNRAEP FQHRCCTDEM VLEQIPQAIH
LAKQSTIIEI QAQRFPEQRF YSRGKTSFSY LAQHLKHKAG TDLLASQSND AVLAEDELDL
INTAEAISAQ PIDWIKSNFP RGTLAGNFLH EIFEHIDFQC SDDWIIEIRR RFKNDYSSLW
QDLLNKYIES FPEEEDAENL LYQSVAEWLK DVLRTPLYQG FRLNQLQQEQ HLSEFPFYLA
LSDRVLAMKR IQQLFAEYGL NMPELLEARS ARYLNGSIDL VYFDGQRYHI ADYKSNYLGD
DLADYRSDSI AQSMSLASYW LQAGLYLVAL HRYLQVKMQD YQIEQHLGGA TYLYLRGMNG
EAEQGYYYWQ PSIEFILRLD AILGYFAEDK IA
//