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Database: UniProt
Entry: R8Y383_ACICA
LinkDB: R8Y383_ACICA
Original site: R8Y383_ACICA 
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
//
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