ID RECA_ACIB5 Reviewed; 349 AA.
AC B7I9U0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 33.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
GN Name=recA; OrderedLocusNames=AB57_2307;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Moraxellaceae; Acinetobacter;
OC Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/JB.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H.,
RA Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A.,
RA Hujer A.M., Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant
RT Acinetobacter baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001182; ACJ42423.1; -; Genomic_DNA.
DR RefSeq; YP_002319659.1; NC_011586.1.
DR ProteinModelPortal; B7I9U0; -.
DR SMR; B7I9U0; 1-328.
DR STRING; 480119.AB57_2307; -.
DR EnsemblBacteria; ACJ42423; ACJ42423; AB57_2307.
DR GeneID; 7045734; -.
DR KEGG; abn:AB57_2307; -.
DR PATRIC; 20698337; VBIAciBau111166_2229.
DR eggNOG; COG0468; -.
DR HOGENOM; HOG000264120; -.
DR KO; K03553; -.
DR OMA; IRRTEWI; -.
DR ProtClustDB; PRK09354; -.
DR BioCyc; ABAU480119:GHQY-3017-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; 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; 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 1 349 Protein RecA.
FT /FTId=PRO_1000193282.
FT NP_BIND 65 72 ATP (By similarity).
SQ SEQUENCE 349 AA; 37891 MW; 2E65AB64ECE13D1F CRC64;
MDENKSKALQ AALSQIEKQF GKNTVMRLGD NTVQAVEAVS TGSLTLDIAL GIGGLPKGRI
IEIYGPESSG KTTMTLQAIA QCQKSGGTCA FIDAEHALDP QYARKLGVDI DNLLVSQPDN
GEQALEIADM LVRSGAIDLI VVDSVAALTP KAEIEGEMGD SHMGLQARLM SQALRKITGN
AKRSNCMVIF INQIRMKIGV MFGSPETTTG GNALKFYASV RLDIRRIGQV KEGDEIVGSE
TKVKVVKNKM APPFKEAIFQ ILYGKGTNQL GELVDLAVQQ DIVQKAGAWY SYQGNKIGQG
KNNVIRYFEE NTQIAEEIER NIREQLLTTG TNGAVQIEDE EEPDLLLES
//
