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Database: UniProt
Entry: F0P1Y4_WEEVC
LinkDB: F0P1Y4_WEEVC
Original site: F0P1Y4_WEEVC 
ID   F0P1Y4_WEEVC            Unreviewed;       453 AA.
AC   F0P1Y4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
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=Weevi_0985 {ECO:0000313|EMBL:ADX67694.1};
OS   Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / CCUG 30538 /
OS   CDC 9751 / IAM 14551 / NBRC 16016 / NCTC 11634 / CL345/78).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Weeksella.
OX   NCBI_TaxID=865938 {ECO:0000313|EMBL:ADX67694.1, ECO:0000313|Proteomes:UP000008641};
RN   [1] {ECO:0000313|EMBL:ADX67694.1, ECO:0000313|Proteomes:UP000008641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC   CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX   PubMed=21475590;
RA   Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E.M., Kopitz M., Rohde M., Goker M., Tindall B.J., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Weeksella virosa type strain (9751).";
RL   Stand. Genomic Sci. 4:81-90(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC   CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX   DOI=10.4056/sigs.1603927;
RA   Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Brambilla E.,
RA   Kopitz M., Rohde M., Goker M., Tindall B., Detter J., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Weeksella virosa type strain (9751T).";
RL   Stand. Genomic Sci. 4:81-90(2011).
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; CP002455; ADX67694.1; -; Genomic_DNA.
DR   RefSeq; WP_013598084.1; NC_015144.1.
DR   AlphaFoldDB; F0P1Y4; -.
DR   STRING; 865938.Weevi_0985; -.
DR   MEROPS; S16.A04; -.
DR   KEGG; wvi:Weevi_0985; -.
DR   eggNOG; COG1066; Bacteria.
DR   HOGENOM; CLU_018264_0_1_10; -.
DR   OrthoDB; 9803906at2; -.
DR   Proteomes; UP000008641; Chromosome.
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:UP000008641};
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          68..215
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   REGION          351..453
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   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   453 AA;  49967 MW;  3032DBBB3BDF5AE0 CRC64;
     MAKIKTAFLC QNCGTQSSQW MGQCKNCGEW NTIVEEVIDK GEDKKVWKNP RHKTSSPVLN
     IREVNPLGET RISTKNAELD RVLGGGIVPG SVILVGGEPG VGKSTLMLQI ALKLNNTKIL
     YVSGEESVNQ VKLRAERIGI ESDECYVLPE TNTQKIFAHA KEIQPQLIII DSVQTLQTAY
     VESSPGSISQ IRETTSELIQ YAKETNTPVI LIGHITKEGV IAGPKILEHM VDVVLQFEGD
     RNHIYRILRA NKNRFGSTAE IGIYEMQGSG LREVTNPSEV LIIKKDEPLS GNAVAATLEG
     VRPMLIEVQA LVSSAVYGTP QRSTTGFDLK RLNMLLAVLE KRAGFRLNLK DVFLNITGGI
     RVDDPALDLA IVAAILSSNE DITVPDNCCF AGEIGLSGEI RAVNRVEQRV TEAEKLGFDA
     IFVSKYNKLK DSDHQIRIIR VSKVEEIYQK LFQ
//
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