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Database: UniProt
Entry: C9XUK7_CROTZ
LinkDB: C9XUK7_CROTZ
Original site: C9XUK7_CROTZ 
ID   C9XUK7_CROTZ            Unreviewed;       336 AA.
AC   C9XUK7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Holliday junction branch migration complex subunit RuvB {ECO:0000256|HAMAP-Rule:MF_00016};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_00016};
GN   Name=ruvB {ECO:0000256|HAMAP-Rule:MF_00016,
GN   ECO:0000313|EMBL:CBA31689.1};
GN   OrderedLocusNames=Ctu_25430 {ECO:0000313|EMBL:CBA31689.1};
OS   Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA31689.1, ECO:0000313|Proteomes:UP000002069};
RN   [1] {ECO:0000313|Proteomes:UP000002069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC   {ECO:0000313|Proteomes:UP000002069};
RX   PubMed=21037008; DOI=10.1128/JB.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT   pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(2011).
CC   -!- FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ)
CC       DNA during genetic recombination and DNA repair, while the RuvA-RuvB
CC       complex plays an important role in the rescue of blocked DNA
CC       replication forks via replication fork reversal (RFR). RuvA
CC       specifically binds to HJ cruciform DNA, conferring on it an open
CC       structure. The RuvB hexamer acts as an ATP-dependent pump, pulling
CC       dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on
CC       either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per
CC       hexamer contact DNA at a time. Coordinated motions by a converter
CC       formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and
CC       nucleotide exchange. Immobilization of the converter enables RuvB to
CC       convert the ATP-contained energy into a lever motion, pulling 2
CC       nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus
CC       driving DNA branch migration. The RuvB motors rotate together with the
CC       DNA substrate, which together with the progressing nucleotide cycle
CC       form the mechanistic basis for DNA recombination by continuous HJ
CC       branch migration. Branch migration allows RuvC to scan DNA until it
CC       finds its consensus sequence, where it cleaves and resolves cruciform
CC       DNA. {ECO:0000256|HAMAP-Rule:MF_00016}.
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=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665, ECO:0000256|HAMAP-
CC         Rule:MF_00016};
CC   -!- SUBUNIT: Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ)
CC       complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters
CC       through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA
CC       strand where it exits the tetramer. Each RuvB hexamer is contacted by
CC       two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this
CC       complex drives branch migration. In the full resolvosome a probable
CC       DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
CC       {ECO:0000256|HAMAP-Rule:MF_00016}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00016}.
CC   -!- DOMAIN: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S)
CC       domains and the C-terminal head (RuvB-H) domain. The head domain binds
CC       DNA, while the ATPase domains jointly bind ATP, ADP or are empty
CC       depending on the state of the subunit in the translocation cycle.
CC       During a single DNA translocation step the structure of each domain
CC       remains the same, but their relative positions change.
CC       {ECO:0000256|HAMAP-Rule:MF_00016}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00016}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00016}.
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DR   EMBL; FN543093; CBA31689.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9XUK7; -.
DR   KEGG; ctu:CTU_25430; -.
DR   PATRIC; fig|693216.3.peg.2413; -.
DR   HOGENOM; CLU_055599_1_0_6; -.
DR   OMA; IHRMSRP; -.
DR   Proteomes; UP000002069; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0000400; F:four-way junction DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_00016; DNA_HJ_migration_RuvB; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041445; AAA_lid_4.
DR   InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008824; RuvB-like_N.
DR   InterPro; IPR008823; RuvB_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00635; ruvB; 1.
DR   PANTHER; PTHR42848; -; 1.
DR   PANTHER; PTHR42848:SF1; HOLLIDAY JUNCTION ATP-DEPENDENT DNA HELICASE RUVB; 1.
DR   Pfam; PF17864; AAA_lid_4; 1.
DR   Pfam; PF05491; RuvB_C; 1.
DR   Pfam; PF05496; RuvB_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00016};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00016};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00016};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00016};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00016};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00016}; Helicase {ECO:0000313|EMBL:CBA31689.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00016};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00016}.
FT   DOMAIN          54..181
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          4..184
FT                   /note="Large ATPase domain (RuvB-L)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   REGION          185..255
FT                   /note="Small ATPAse domain (RuvB-S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   REGION          258..336
FT                   /note="Head domain (RuvB-H)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         131..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         221
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         294
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         313
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         318
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
SQ   SEQUENCE   336 AA;  37293 MW;  CA81351EE84DA706 CRC64;
     MIEADRLVAP GSIVAEEVAD RAMRPKLLDE YIGQPQVRSQ MEIFIQAAKL RGDALDHLLI
     FGPPGLGKTT LANIVANEMG VNLRTTSGPV LEKAGDLAAM LTNLEPHDVL FIDEIHRLSP
     VVEEVLYPAM EDYQLDIMIG EGPAARSIKI DLPPFTLIGA TTRAGSLTSP LRDRFGIVQR
     LEFYQVADLQ HIVSRSARHM GLEMNDEASF EVAKRSRGTP RIANRLLRRV RDFAEVRHDG
     VINQHVASLA LDMLNVDAEG FDYMDRKLLL AVIDKFFGGP VGLDNLAAAI GEERETIEDV
     LEPFLIQQGF LQRTPRGRMA TTRAWNHFGI TPPQMP
//
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