ID A0A2C5UZK1_RAOPL Unreviewed; 460 AA.
AC A0A2C5UZK1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555};
GN Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN ORFNames=DN603_00560 {ECO:0000313|EMBL:RWT26084.1}, NCTC12998_02950
GN {ECO:0000313|EMBL:VFS66134.1}, SAMEA2273876_03774
GN {ECO:0000313|EMBL:SBM33953.1};
OS Raoultella planticola (Klebsiella planticola).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX NCBI_TaxID=575 {ECO:0000313|EMBL:RWT26084.1, ECO:0000313|Proteomes:UP000288843};
RN [1] {ECO:0000313|EMBL:SBM33953.1, ECO:0000313|Proteomes:UP000078124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2880STDY5682802 {ECO:0000313|EMBL:SBM33953.1,
RC ECO:0000313|Proteomes:UP000078124}, and NCTC12998
RC {ECO:0000313|EMBL:VFS66134.1, ECO:0000313|Proteomes:UP000345637};
RG Pathogen Informatics;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RWT26084.1, ECO:0000313|Proteomes:UP000288843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GEO_47_Down_B {ECO:0000313|EMBL:RWT26084.1,
RC ECO:0000313|Proteomes:UP000288843};
RA Mathys D.A., Mollenkopf D.F., Feicht S.M., Adams R.J., Albers A.L.,
RA Stuever D.M., Daniels J.B., Wittum T.E.;
RT "Carbapenemase-producing Enterobacteriaceae present in wastewater treatment
RT plant effluent and nearby surface waters in the US.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase involved in processing of recombination
CC intermediates, plays a role in repairing DNA breaks. Stimulates the
CC branch migration of RecA-mediated strand transfer reactions, allowing
CC the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA
CC in the presence of ADP but not other nucleotides, has ATPase activity
CC that is stimulated by ssDNA and various branched DNA structures, but
CC inhibited by SSB. Does not have RecA's homology-searching function.
CC {ECO:0000256|RuleBase:RU003555}.
CC -!- FUNCTION: Plays a role in repairing double-strand DNA breaks, probably
CC involving stabilizing or processing branched DNA or blocked replication
CC forks. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC -!- DOMAIN: The middle region has homology to RecA with ATPase motifs
CC including the RadA KNRFG motif, while the C-terminus is homologous to
CC Lon protease. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555}.
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DR EMBL; QKOX01000001; RWT26084.1; -; Genomic_DNA.
DR EMBL; FLAC01000016; SBM33953.1; -; Genomic_DNA.
DR EMBL; CAADJE010000023; VFS66134.1; -; Genomic_DNA.
DR RefSeq; WP_004857671.1; NZ_VLNM01000006.1.
DR GeneID; 72407267; -.
DR Proteomes; UP000078124; Unassembled WGS sequence.
DR Proteomes; UP000288843; Unassembled WGS sequence.
DR Proteomes; UP000345637; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR CDD; cd01121; RadA_SMS_N; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01498; RadA_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004504; DNA_repair_RadA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR041166; Rubredoxin_2.
DR NCBIfam; TIGR00416; sms; 1.
DR PANTHER; PTHR32472; DNA REPAIR PROTEIN RADA; 1.
DR PANTHER; PTHR32472:SF10; DNA REPAIR PROTEIN RADA-LIKE PROTEIN; 1.
DR Pfam; PF13481; AAA_25; 1.
DR Pfam; PF13541; ChlI; 1.
DR Pfam; PF18073; Rubredoxin_2; 1.
DR PRINTS; PR01874; DNAREPAIRADA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Zinc {ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 73..221
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 357..460
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 258..262
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 460 AA; 49498 MW; F656258626FBF5F8 CRC64;
MAKAPKRAFV CNECGADYPR WQGQCSACHA WNTITEVRIA ASPQVARNER LTGYAGNAGA
SKVQKLSEIS LEALPRFSTG FKEFDRVLGG GVVPGSAILI GGSPGAGKST LLLQTLCRLS
ENMKTLYVTG EESLQQVAMR AHRLGLPTAN LNMLSETSIE QICQIADDEK PQLMVIDSIQ
VMHMADVQSS PGSVAQVRET AAYLTRFAKT RDVAIIMVGH VTKDGSLAGP KVLEHCIDCS
VLLDGDADSR FRTLRSHKNR FGAVNELGVF AMTEQGLREI SNPSAIFLSR GDEVTSGSSV
MVVWEGTRPL LVEIQALVDH SMMSNPRRVA VGLEQNRLAI LLAVLHRHGG LQMADQDVFV
NVVGGVKVAE TSADLALLLA MVSSLRDRPL PHDLVVFGEV GLSGEIRPVP SGQERISEAA
KHGFRRAIVP AANVPKKAPE GMQIFGVKKL SDALSVFDDL
//
