RECA_CAMLA
ID RECA_CAMLA Reviewed; 344 AA.
AC Q93R37; Q93R36;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
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};
OS Campylobacter lari.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=201;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35221 / DSM 11375 / JCM 2530 / LMG 8846 / NCTC 11352;
RA Honda M., Matsushita S., Murayama O., Millar B.C., Moore J.E., Matsuda M.;
RT "Cloning and sequence analysis of the recA gene of Campylobacter lari
RT JCM2530.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCTC 12894 / A692/85;
RA Matsuda M., Honda M., Matsushita S., Matsui T., Murayama O., Millar B.C.,
RA Moore J.E.;
RT "Cloning and sequence analysis of the recA gene of urease-positive
RT thermophilic Campylobacter.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
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; AB067767; BAB62716.1; -; Genomic_DNA.
DR EMBL; AB067768; BAB62717.1; -; Genomic_DNA.
DR RefSeq; WP_039617275.1; NZ_UFVM01000002.1.
DR AlphaFoldDB; Q93R37; -.
DR SMR; Q93R37; -.
DR OrthoDB; 1080436at2; -.
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; IPR020584; DNA_recomb/repair_RecA_CS.
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; PS00321; RECA_1; 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; SOS response.
FT CHAIN 1..344
FT /note="Protein RecA"
FT /id="PRO_0000122679"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT VARIANT 101
FT /note="K -> R (in strain: NCTC 12894)"
FT VARIANT 105
FT /note="D -> N (in strain: NCTC 12894)"
FT VARIANT 176
FT /note="E -> K (in strain: NCTC 12894)"
FT VARIANT 219
FT /note="S -> A (in strain: NCTC 12894)"
FT VARIANT 342..343
FT /note="GD -> EGE (in strain: NCTC 12894)"
SQ SEQUENCE 344 AA; 37161 MW; 5CF9C3AD5E045C52 CRC64;
MDDNKRKSLD AALKSLDKTF GKGTILRLGD KEVEKIDSIP TGSVGLDLAL GIGGVPKGRI
IEIYGPESSG KTTLTLHIIA ECQKKGGVCA FIDAEHALDV KYAKDLGVDT ENLYISQPDF
GEQALEIVET IARSGAIDLI VVDSVAALTP KAEIEGDMGD QHVGLQARLM SQALRELTGI
VHKMNTTVIF INQIRMKIGM MGYGTPETTT GGNALKFYSS VRLDVRKTAT LKQNDEPIGN
RVKVKVAKNK VAPPFKQAEF DVMFGEGVSR EGELIDYGVK LDIIDKSGAW FSYKASKLGQ
GRENAKAFLK ENPAIADEIT QAIQNSIGID SMILGAKEDD EGDE