RECA_GLUOX
ID RECA_GLUOX Reviewed; 345 AA.
AC P48289; Q5FQT2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; OrderedLocusNames=GOX1522;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liu Y.T.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC DNA, and the ATP-dependent hybridization of homologous single-stranded
CC DNAs. It interacts with LexA causing its activation and leading to its
CC autocatalytic cleavage. {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; U21001; AAA73517.1; -; Genomic_DNA.
DR EMBL; CP000009; AAW61264.1; -; Genomic_DNA.
DR RefSeq; WP_011253049.1; NZ_LT900338.1.
DR AlphaFoldDB; P48289; -.
DR SMR; P48289; -.
DR STRING; 290633.GOX1522; -.
DR PRIDE; P48289; -.
DR EnsemblBacteria; AAW61264; AAW61264; GOX1522.
DR KEGG; gox:GOX1522; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_1_2_5; -.
DR OMA; DYGEQAL; -.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00268; RecA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..345
FT /note="Protein RecA"
FT /id="PRO_0000122720"
FT REGION 326..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT CONFLICT 32..35
FT /note="VETN -> EQAD (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="I -> L (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="F -> V (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="D -> E (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="A -> C (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="A -> R (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..193
FT /note="IR -> MG (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="R -> H (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="G -> A (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 308..309
FT /note="EH -> DD (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="A -> S (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..323
FT /note="AE -> SD (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..328
FT /note="LS -> VA (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 333..334
FT /note="TD -> VG (in Ref. 1; AAA73517)"
FT /evidence="ECO:0000305"
FT CONFLICT 337..345
FT /note="PDADGTPED -> GDEASSDD (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 37256 MW; 5FB1AC98638F2DBE CRC64;
MDKTKALEGA LSQIERAFGK GSIMRMGQRP KVETNVISTG SIGLDIALGI GGMPRGRIVE
IYGPESSGKT TLALHVLAEA QKKGGTVAFI DAEHALDPGY ARKLGVNIDD LLLSQPDAGE
QALEIADTLV RSGAVDVLVV DSVAALVPRA ELEGDMGDSH VGLHARLMSQ ALRKLTGTVS
RSNTLVIFLN QIRMKIGVMF GNPETTTGGN ALKFYSSIRL DIRRIGSIKD KDEVVGNQTR
VKVVKNKMAP PFRQVEFDIM YGEGISKMGE LLDLGVKGNI VEKSGAWFSF DSQRIGQGRE
NAKQFLREHP EMASEIERRI RAEAGVLSDA LMTDPEPDAD GTPED
