ID A0A0B8T4J5_9SPHI Unreviewed; 461 AA.
AC A0A0B8T4J5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=DI53_1462 {ECO:0000313|EMBL:KGE14788.1};
OS Sphingobacterium deserti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE14788.1, ECO:0000313|Proteomes:UP000031802};
RN [1] {ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RA Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C.,
RA Zhang W.;
RT "Whole-Genome optical mapping and complete genome sequence of
RT Sphingobacterium deserti sp. nov., a new spaces isolated from desert in the
RT west of China.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGE14788.1, ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RX PubMed=25830331;
RA Teng C., Zhou Z., Molnar I., Li X., Tang R., Chen M., Wang L., Su S.,
RA Zhang W., Lin M.;
RT "Whole-Genome Optical Mapping and Finished Genome Sequence of
RT Sphingobacterium deserti sp. nov., a New Species Isolated from the Western
RT Desert of China.";
RL PLoS ONE 10:E0122254-E0122254(2015).
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}.
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:KGE14788.1}.
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DR EMBL; JJMU01000023; KGE14788.1; -; Genomic_DNA.
DR RefSeq; WP_037497173.1; NZ_JJMU01000023.1.
DR AlphaFoldDB; A0A0B8T4J5; -.
DR STRING; 1229276.DI53_1462; -.
DR PATRIC; fig|1229276.3.peg.1513; -.
DR eggNOG; COG1066; Bacteria.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000031802; 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|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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW Reference proteome {ECO:0000313|Proteomes:UP000031802};
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..461
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 461 AA; 50539 MW; 2E24630927802670 CRC64;
MAKAKSTYFC QQCGYESAKW LGQCPSCKQW NSFVEEVVEK TSSKVPEWRS TTAPASTRRT
NKAAVINEIV YQDEQRLASP DREFNRVLGG GIVPGSLVLI GGEPGIGKST LMLQLALSIP
AVKTLYISGE ESEQQIKMRA ERLVQNSTAN CYILTETSTQ NIFKQIEVVQ PDIVVIDSIQ
TLHSSQIESA PGSVSQVREC TAELLRFAKE TSTPVFIVGH ITKDGSIAGP KVLEHMVDTV
LQFEGDRHHV YRILRSVKNR FGSSSELGIY EMQGSGLREV SNPSEIMLSQ REEPVGGVAI
AAMLEGVRPI MIEVQALVSN SAFGTPQRTS TGFDTKRLSM LLAVLEKRFG FRLSAQDVFL
NIAGGLRVED PAIDLAVIAA LISSQQDIPL SSQLTFAGEV GLSGEIRAVN RIEQRIAEAE
KLGFEGIFIS KYNTKGLDAK KYNIAIRPMA TLEDLFRALF G
//