ID RECA_VIBF1 Reviewed; 348 AA.
AC Q5E7G6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 29-MAY-2013, entry version 62.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=VF_0535;
OS Vibrio fischeri (strain ATCC 700601 / ES114).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium
RT with pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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 -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000020; AAW85030.1; -; Genomic_DNA.
DR RefSeq; YP_203918.1; NC_006840.2.
DR ProteinModelPortal; Q5E7G6; -.
DR SMR; Q5E7G6; 1-328.
DR STRING; 312309.VF_0535; -.
DR PRIDE; Q5E7G6; -.
DR EnsemblBacteria; AAW85030; AAW85030; VF_0535.
DR GeneID; 3277128; -.
DR KEGG; vfi:VF_0535; -.
DR PATRIC; 20111584; VBIVibFis127983_0527.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; DIMLMIQ; -.
DR ProtClustDB; PRK09354; -.
DR BioCyc; AFIS312309:GIWP-554-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 Reference proteome; SOS response.
FT CHAIN 1 348 Protein RecA.
FT /FTId=PRO_0000122892.
FT NP_BIND 65 72 ATP (By similarity).
SQ SEQUENCE 348 AA; 37587 MW; FB374E5D3C908B64 CRC64;
MDDNKKKALA AALGQIEKQF GKGSIMKLGD NRTMDVETVS TGSLSLDIAL GAGGLPMGRI
VEIFGPESSG KTTLTLELIA AAQREGKTCA FIDAEHALDP VYAKKLGVNI DELLVSQPDT
GEQALEICDA LARSGAVDVM VIDSVAALTP KAEIEGEMGD SHMGLQARML SQAMRKLTGN
LKQSNCMAIF INQIRMKIGV MFGNPETTTG GNALKFYASV RLDIRRTGAV KDGDEVVGNE
TRIKVVKNKI AAPFKQAETQ IMYGQGFNRE GELIDLGVKH KLVDKAGAWY SYNGDKIGQG
KANASKFMRE NTEVAAELDK KLREMLLTPA EEKPETDAAP EIEENEEF
//
