RECA_MYCGS
ID RECA_MYCGS Reviewed; 419 AA.
AC Q9F414;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein RecA;
DE AltName: Full=Recombinase A;
DE Contains:
DE RecName: Full=Mga RecA intein;
DE Flags: Fragment;
GN Name=recA;
OS Mycobacterium gastri.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1777;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HB4389;
RX PubMed=11034333; DOI=10.1016/s0014-5793(00)01944-x;
RA Saves I., Laneelle M.-A., Daffe M., Masson J.-M.;
RT "Inteins invading mycobacterial RecA proteins.";
RL FEBS Lett. 480:221-225(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000305}.
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DR EMBL; AJ251715; CAC09591.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F414; -.
DR PRIDE; Q9F414; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease 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:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR Gene3D; 3.10.28.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF03161; LAGLIDADG_2; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Autocatalytic cleavage; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding;
KW Protein splicing; SOS response.
FT CHAIN <1..9
FT /note="Protein RecA, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030257"
FT CHAIN 10..377
FT /note="Mga RecA intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030258"
FT CHAIN 378..>419
FT /note="Protein RecA, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030259"
FT NON_TER 1
FT NON_TER 419
SQ SEQUENCE 419 AA; 46602 MW; 4BB42A3BC12941E6 CRC64;
RDKIGVMFGC GSWYTNVTLA DGSTEKLGKI VNQKMDVEVL SYDFESGQIV PRRVTNWFNN
GKAEEFLHFK VDRAGSGTGR GHASLAMTRN HLIRTPVGWR EAEDINVGDR VMLAQPRLLS
DQQWEIVLGS LMGDGCLSPP VRQDSESARL RIGHGAQQSA YFDWKVSLLA NIPHSRTVNG
KGAAFVDFSP LAELHELRSA VYLGDGKKFL SEEYLKGLTP LSLAIWYMDD GSFSLRSKGL
QQRTQGGSGR IEICVEAMSE GSQVRLRDYL HDTHGLDVRL RKAGAAAKAV LVFSTAATAK
FQQLVAPYMA PCMAYKLLPR FHGRSMVTPQ FVEPIMELMP ARVTEIESKT DYPIMSRFDI
EVEGSHNYFA DGVMVHNSPE TTTGGKALKF YASVRMDVQR IETLKDGTNT VDNRTRVKI