ID RECA_TROWT Reviewed; 437 AA.
AC P65981; Q83MS9; Q83NC6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 29-MAY-2013, entry version 62.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=TWT_611;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micrococcineae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of
CC single-stranded DNA, the ATP-dependent uptake of single-stranded
CC DNA by duplex DNA, and the ATP-dependent hybridization of
CC homologous single-stranded DNAs. It interacts with LexA causing
CC its activation and leading to its autocatalytic cleavage (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the RecA family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO44708.1; Type=Erroneous initiation;
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DR EMBL; AE014184; AAO44708.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_787739.1; NC_004572.3.
DR ProteinModelPortal; P65981; -.
DR SMR; P65981; 8-331.
DR STRING; 203267.TWT611; -.
DR PRIDE; P65981; -.
DR EnsemblBacteria; AAO44708; AAO44708; TWT_611.
DR GeneID; 1482600; -.
DR KEGG; twh:TWT611; -.
DR PATRIC; 23997843; VBITroWhi72342_0783.
DR eggNOG; COG0468; -.
DR KO; K03553; -.
DR OMA; TRKGAWY; -.
DR ProtClustDB; PRK09354; -.
DR BioCyc; TWHI203267:GJDK-650-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003684; F:damaged DNA binding; IEA:HAMAP.
DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:HAMAP.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:HAMAP.
DR GO; GO:0006310; P:DNA recombination; IEA:HAMAP.
DR GO; GO:0006281; P:DNA repair; IEA:HAMAP.
DR GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR Gene3D; 3.30.250.10; -; 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; IPR020588; DNA_recomb_RecA/RadB_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR22942:SF1; PTHR22942:SF1; 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; Complete proteome; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding;
KW SOS response.
FT CHAIN 1 437 Protein RecA.
FT /FTId=PRO_0000122887.
FT NP_BIND 69 76 ATP (By similarity).
SQ SEQUENCE 437 AA; 46450 MW; 969186E5C5F390D8 CRC64;
MSSNDQINRT RALELALANI DRQYGKGAVM RMNDAQKAYI DVIPTGSIAL DYALGVGGLP
RGRIVEIYGP ESSGKTTLTL HAIASVQRAG GIAAFIDAEH ALDPEYAKKL GVDIDALLVS
QPDSGEQALE ISDMLIRSTA IDLIVIDSVA ALVPRAELEG DMGDMHVGLQ ARLMSQALRK
ITSGLNQTGT TAIFINQLRE KVGVFFGSPE TTPGGRALKF YASVRLDIRR VETIKQGTEA
VGNRTRVKVV KNKVAPPFKQ AEFDVLYGVG ISRESGLIDF AVDRGIIKKS GSWYVYGDDQ
LGQGKENARR FLLENKSVAD EIENKIISLL GFRSNEFGDL PDHDAAVRTS PDTNSRKVSG
TGAVHTTSGS PSAGKGTASG AVNNSRDSTG GDTPAGQGPL NLSVNRDVST DTVSSKISDA
THNQKPAGNG KSVKRKG
//