RECA_NEIMU
ID RECA_NEIMU Reviewed; 274 AA.
AC Q59619; O86398;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
DE Flags: Fragment;
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268};
OS Neisseria mucosa.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LNP 405;
RX PubMed=8995060; DOI=10.1007/bf02202111;
RA Feil E., Zhou J., Maynard Smith J., Spratt B.G.;
RT "A comparison of the nucleotide sequences of the adk and recA genes of
RT pathogenic and commensal Neisseria species: evidence for extensive
RT interspecies recombination within adk.";
RL J. Mol. Evol. 43:631-640(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-254.
RC STRAIN=Vedros M1801;
RA Smith N.H., Donovan G.M., Carpenter A., Spratt B.G.;
RT "Do sexual bacteria have species?";
RL Submitted (JAN-1998) 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; U57908; AAB49197.1; -; Genomic_DNA.
DR EMBL; AJ223875; CAA11606.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59619; -.
DR SMR; Q59619; -.
DR STRING; 435832.HMPREF0604_00497; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
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..>274
FT /note="Protein RecA"
FT /id="PRO_0000122779"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT VARIANT 42
FT /note="F -> L (in strain: Vedros M1801)"
FT VARIANT 49
FT /note="K -> N (in strain: Vedros M1801)"
FT VARIANT 115
FT /note="V -> I (in strain: Vedros M1801)"
FT VARIANT 245
FT /note="V -> I (in strain: Vedros M1801)"
FT NON_TER 1
FT NON_TER 274
SQ SEQUENCE 274 AA; 29612 MW; 120614DB34447199 CRC64;
SIMKMDGSQQ EENLDVISTG SLGVDLALGV GGLPRGRVVE IFGPESSGKT TLCLEAIAQC
QKNGGICAFI DAEHAFDPIY ARKLGVKVEE LYLSQPDTGE QALEICDTLV RSGGVDMVVV
DSVAALVPKA EIEGEMGDSH VGLQARLMSQ ALRKLTGHIK RTNTLVVFIN QIRMKIGVMF
GSPETTTGGN ALKFYASVRL DIRRTGQIKK GDDVIGNETK VKVIKNKVAP PFRQAEFDIL
YGEGVSWEGE LIDLGVKYDI VEKSGAWYSY NGAK