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RECA_THEMA
ID   RECA_THEMA              Reviewed;         356 AA.
AC   P36203;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 146.
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}; OrderedLocusNames=TM_1859;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7929298; DOI=10.1016/s0021-9258(18)47335-8;
RA   Wetmur J.G., Wong D.M., Ortiz B., Tong J., Reichert F., Gelfand D.H.;
RT   "Cloning, sequencing, and expression of RecA proteins from three distantly
RT   related thermophilic eubacteria.";
RL   J. Biol. Chem. 269:25928-25935(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; L23425; AAA27417.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD36921.1; -; Genomic_DNA.
DR   PIR; D55020; D55020.
DR   RefSeq; NP_229655.1; NC_000853.1.
DR   RefSeq; WP_004082410.1; NZ_CP011107.1.
DR   PDB; 3HR8; X-ray; 1.95 A; A=1-356.
DR   PDBsum; 3HR8; -.
DR   AlphaFoldDB; P36203; -.
DR   SMR; P36203; -.
DR   STRING; 243274.THEMA_04875; -.
DR   EnsemblBacteria; AAD36921; AAD36921; TM_1859.
DR   KEGG; tma:TM1859; -.
DR   eggNOG; COG0468; Bacteria.
DR   InParanoid; P36203; -.
DR   OMA; DYGEQAL; -.
DR   OrthoDB; 1080436at2; -.
DR   Proteomes; UP000008183; Chromosome.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA recombination;
KW   DNA repair; DNA-binding; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   CHAIN           1..356
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122878"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT   HELIX           5..22
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           47..52
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          54..59
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          62..69
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           74..87
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           103..109
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           124..136
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          141..146
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           154..157
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           168..185
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          190..199
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          201..205
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           213..220
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          222..235
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          238..254
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          259..265
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           272..282
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          285..289
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          292..296
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   STRAND          302..307
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           308..318
FT                   /evidence="ECO:0007829|PDB:3HR8"
FT   HELIX           320..333
FT                   /evidence="ECO:0007829|PDB:3HR8"
SQ   SEQUENCE   356 AA;  38798 MW;  A2B70853C26C95FD CRC64;
     MPEEKQKKSV LEKALKRIEE NFGKGSIMIL GDETQVQPVE VIPTGSLAID IATGVGGYPR
     GRIVEIFGQE SSGKTTLALH AIAEAQKMGG VAAFIDAEHA LDPVYAKNLG VDLKSLLISQ
     PDHGEQALEI VDELVRSGVV DLIVVDSVAA LVPRAEIEGA MGDMQVGLQA RLMSQALRKI
     AGSVNKSKAV VIFTNQIRMK IGVMFGSPET TTGGLALKFY ATMRMEVRRG EPIKEGKDVI
     GNVISVKIVK NKVAPPFKTA QTYIIYGKGI DREYELFNIA VNEGIVDRKG SWYYYTTLKG
     EEVSLGQGSS NAVQFLKDNP EIAGEIERRI REKYGLLSVE KEEQRKEKKS SGEEAS
 
 
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