RECA_RHOBA
ID RECA_RHOBA Reviewed; 375 AA.
AC Q7UJJ0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=RB11863;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294154; CAD77268.1; -; Genomic_DNA.
DR RefSeq; NP_870193.1; NC_005027.1.
DR RefSeq; WP_011123464.1; NC_005027.1.
DR AlphaFoldDB; Q7UJJ0; -.
DR SMR; Q7UJJ0; -.
DR STRING; 243090.RB11863; -.
DR EnsemblBacteria; CAD77268; CAD77268; RB11863.
DR KEGG; rba:RB11863; -.
DR PATRIC; fig|243090.15.peg.5722; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_0; -.
DR InParanoid; Q7UJJ0; -.
DR OMA; DYGEQAL; -.
DR OrthoDB; 1080436at2; -.
DR Proteomes; UP000001025; 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; 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; 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..375
FT /note="Protein RecA"
FT /id="PRO_0000122816"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 375 AA; 39959 MW; BBDBB97A0B8FC113 CRC64;
MVKKPRMATP AASKGVKLDP GMKTILEKEP GLKTTLQQIE KSFGDGAIMP LGASQKLTID
CISTGSLSLD MALGGKGIPR GRIIEVFGPE SSGKTTLALH IGAEAQKSGG IAAIIDAEHA
FDPSWAKKLG VELDSLLVSQ PSSGEEAMQI CEMLVKSNAV DVIIIDSVAA LVPKAELEGE
IGDSHVGLQA RLMSQSMRKL TGAIAKSKSA VVFINQIREK VGVMFGSPET TPGGRALKFY
CSCRIDVRRI GSLKDGEEQV GQRVKAKIVK NKVAPPFRIA EFDMMHSNGI SFEGDLLDLG
TENKVVNRSG SWFKYGDTYL GQGKEKARNF LIENPDVSDE IKQKVLAAGG FVAPLEVDAD
ESEEAVEDGE AVANS