ID RECA_METCA Reviewed; 347 AA.
AC Q60BS8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 29-MAY-2013, entry version 60.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=MCA0387;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E.,
RA Ravel J., Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R.,
RA Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J.,
RA Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S.,
RA Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R.,
RA Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
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.
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DR EMBL; AE017282; AAU90485.1; -; Genomic_DNA.
DR RefSeq; YP_112918.1; NC_002977.6.
DR ProteinModelPortal; Q60BS8; -.
DR SMR; Q60BS8; 1-329.
DR STRING; 243233.MCA0387; -.
DR PRIDE; Q60BS8; -.
DR EnsemblBacteria; AAU90485; AAU90485; MCA0387.
DR GeneID; 3104748; -.
DR KEGG; mca:MCA0387; -.
DR PATRIC; 22604519; VBIMetCap22254_0401.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; TRKGAWY; -.
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 1 347 Protein RecA.
FT /FTId=PRO_0000122756.
FT NP_BIND 66 73 ATP (By similarity).
SQ SEQUENCE 347 AA; 37068 MW; 91E823A970397667 CRC64;
MDENKRKALG AALSQIEKQF GKGSVMRMGD VAAVRDIDVI PTGSLALDIA LGCGGLPRGR
IVEIYGPESS GKTTLTLEVI AQAQKTGGVA AFVDAEHALD PVYAEKIGVN LDDLLVSQPD
TGEQALEIAD VLVRSGGVDV VVIDSVAALT PKAELEGEMG DSHMGLQARL MSQALRKLTA
NIKRSNTLVI FINQIRMKIG VMFGNPETTT GGNALKFYAS VRLDIRRSGA IKNGDEVIGN
ETRVKVVKNK VAPPFRTADF EILYGEGISR EGELIDLGVN HDIVQKSGSW YSYGGDRIGQ
GKDNVRIYLK EHPEVAAAIE AAVREKALAG FQHAPSAERA ALEESGF
//
