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Database: UniProt
Entry: D1CBU0_THET1
LinkDB: D1CBU0_THET1
Original site: D1CBU0_THET1 
ID   D1CBU0_THET1            Unreviewed;       460 AA.
AC   D1CBU0;
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=Tter_1348 {ECO:0000313|EMBL:ACZ42255.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Chloroflexota; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ42255.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ42255.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H.,
RA   Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M.,
RA   Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA   Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(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; CP001825; ACZ42255.1; -; Genomic_DNA.
DR   RefSeq; WP_012875290.1; NC_013525.1.
DR   AlphaFoldDB; D1CBU0; -.
DR   STRING; 525904.Tter_1348; -.
DR   MEROPS; S16.A04; -.
DR   KEGG; ttr:Tter_1348; -.
DR   eggNOG; COG1066; Bacteria.
DR   HOGENOM; CLU_018264_0_1_0; -.
DR   OrthoDB; 9803906at2; -.
DR   Proteomes; UP000000323; 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:ACZ42255.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW   ECO:0000256|RuleBase:RU003555};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_01498}; Transferase {ECO:0000313|EMBL:ACZ42255.1};
KW   Zinc {ECO:0000256|RuleBase:RU003555};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT   DOMAIN          67..216
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   REGION          352..460
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT   MOTIF           253..257
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT   BINDING         96..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   460 AA;  49734 MW;  2270184753097FDB CRC64;
     MSKTRSRTVY VCNSCGNVSP KWQGRCPECG QWNTYVETVE QPAPTTSGIS TNVTSRPRRL
     KDVSADDIHR IHVPMPEVNR VLGGGIVSGS LVLIGGDPGV GKSTLLLQLC CLLCDQLSTV
     LYVSGEESIE QIRLRASRLG RIPDNLWAVS ETSLEAILNL IEEQSPSLVI IDSIQTIYSE
     NIESAAGSVS QVRDCTMALM LTAKSRNIPM FIVGHVTKEG AIAGPKVLEH IVDTVLYLEG
     DRAHQYRLLR AAKNRYGSTN EVGVFEMTQE GLIDVPNPSE VFLSERPEDT VGSSIAVLLE
     GSRPLLVELQ ALAIHNPTGI PRRTSNGLDY NRLLLLIAVL TKRVGLKLAD QDIYVNVVGG
     LRLDEPSSDL AVAVAIASSA LNRPVREDTI FVGEVGLSGE LRSVPNIDRR ISEAASLGFK
     RAVCAPVKKN AQKINSIQIV QAKTLAEAIG KSLYPPAGKD
//
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