ID D1C7V2_SPHTD Unreviewed; 462 AA.
AC D1C7V2;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 OrderedLocusNames=Sthe_0497 {ECO:0000313|EMBL:ACZ37935.1};
OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ37935.1, ECO:0000313|Proteomes:UP000002027};
RN [1] {ECO:0000313|Proteomes:UP000002027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC {ECO:0000313|Proteomes:UP000002027};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA Goeker M., Klenk H.P., Eisen J.A.;
RT "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ37935.1, ECO:0000313|Proteomes:UP000002027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC {ECO:0000313|Proteomes:UP000002027};
RX PubMed=21304676;
RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfohalobium retbaense type strain
RT (HR(100)).";
RL Stand. Genomic Sci. 2:38-48(2010).
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; CP001823; ACZ37935.1; -; Genomic_DNA.
DR RefSeq; WP_012870982.1; NC_013523.1.
DR AlphaFoldDB; D1C7V2; -.
DR STRING; 479434.Sthe_0497; -.
DR MEROPS; S16.A04; -.
DR KEGG; sti:Sthe_0497; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_0; -.
DR InParanoid; D1C7V2; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000002027; Chromosome 1.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; 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|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
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}; Methyltransferase {ECO:0000313|EMBL:ACZ37935.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW Reference proteome {ECO:0000313|Proteomes:UP000002027};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Transferase {ECO:0000313|EMBL:ACZ37935.1};
KW Zinc {ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 66..215
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..462
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 252..256
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT COMPBIAS 39..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 462 AA; 49135 MW; 68AA06A91ABC5A31 CRC64;
MSKARTKFVC QNCGMETPAY YGRCPQCGTW GSMVETVEAR GPARERRERG MPATRPARLS
EVTSAEERRK VVPIGEFNRV LGGGLVPGSL VLLGGDPGVG KSTLLLQVAG LLAPSAGPVV
YVSAEESTQQ IKLRADRLGI TADDLYLLSE TNLEAALDAV DPVKPGLLIV DSIQTVYLDD
LTSAAGSVSQ VRECTARLMQ YAKPRHLPVF IVGHVTKEGA IAGPRVLEHM VDAVLYLEGE
RYHQYRVLRA VKNRFGSTDE VGVFAMTGDG MQEVANPSEA FLQERSPDTH GSAVGVTLEG
TRPILVEVQA LTSNSAFGLP RRTANGFDNN RLQMLVAVLS KRVGLGLGSQ DIYVNIVGGL
RIAEPAADLA VVTAIASSYR ERPVDPNTVV IGEVGLSGEL RSVNQIERRL NEASKLGFAR
AVVPAPGGRR QLPKVSGIEV IPAASAAEAI EMALVHGPVG GS
//
