ID   RECA_AZOL4              Reviewed;         359 AA.
AC   P62209; G7Z545;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 92.
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=AZOLI_1478;
OS   Azospirillum lipoferum (strain 4B).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHASE VARIATION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=4B;
RX   PubMed=15251210; DOI=10.1111/j.1574-6968.2004.tb09660.x;
RA   Vial L., Pothier J.F., Normand P., Moenne-Loccoz Y., Bally R.,
RA   Wisniewski-Dye F.;
RT   "Construction of a recA mutant of Azospirillum lipoferum and involvement of
RT   recA in phase variation.";
RL   FEMS Microbiol. Lett. 236:291-299(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B;
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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       ECO:0000269|PubMed:15251210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC   -!- DISRUPTION PHENOTYPE: Cells are more sensitive to UV and MMS, and have
CC       no detectable recombinase activity. They are still able to generate
CC       phase variants, as do wild-type cells, and surprisingly do so at a 10-
CC       fold greater rate. Phase variants irreversibly lose the ability to
CC       swim, and undergo changes in their sugar assimilation profile.
CC       {ECO:0000269|PubMed:15251210}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00268}.
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DR   EMBL; AY422794; AAR00257.1; -; Genomic_DNA.
DR   EMBL; FQ311868; CBS86779.1; -; Genomic_DNA.
DR   RefSeq; WP_014247796.1; NC_016622.1.
DR   AlphaFoldDB; P62209; -.
DR   SMR; P62209; -.
DR   STRING; 862719.AZOLI_1478; -.
DR   EnsemblBacteria; CBS86779; CBS86779; AZOLI_1478.
DR   KEGG; ali:AZOLI_1478; -.
DR   HOGENOM; CLU_040469_1_2_5; -.
DR   OMA; DYGEQAL; -.
DR   OrthoDB; 1080436at2; -.
DR   Proteomes; UP000005667; 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   ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT   CHAIN           1..359
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122645"
FT   BINDING         77..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT   CONFLICT        173..175
FT                   /note="SHV -> AMS (in Ref. 1; AAR00257)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349..359
FT                   /note="PEADGEASTPE -> RKPTAKPPHRSEVPSEQEARC (in Ref. 1;
FT                   AAR00257)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   359 AA;  38137 MW;  13B27BE817A3A0F2 CRC64;
     MSSAQLRLVE KDSMDKQKAL DAALSQIERA FGKGSIMKLG ARENLVETEV ISTGSLGLDI
     ALGIGGLPKG RIVEIYGPES SGKTTLALHA IAQAQKAGGT CAFVDAEHAL DPSYARKLGV
     NIDELLISQP DAGEQALEIA DTLVRSGAID VLVVDSVAAL VPRAELEGEM GDSHVGLHAR
     LMSQALRKLT GSISKSNCLV IFINQIRLKI GVMFGNPETT TGGNALKFYA SVRLDIRRIG
     SIKDRDTVVG NQTRVKVVKN KMAPPFRVVE FDIMYGEGVS KVGELLDLGI QAGVVDKSGA
     WFSYDGTRIG QGRENAKTYL RNNPEMADAI EAKIRGNAGL VADAMMGTPE ADGEASTPE