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Database: UniProt
Entry: I0R2Z7_9MICO
LinkDB: I0R2Z7_9MICO
Original site: I0R2Z7_9MICO 
ID   I0R2Z7_9MICO            Unreviewed;       362 AA.
AC   I0R2Z7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Protein RecA {ECO:0000256|ARBA:ARBA00015553, ECO:0000256|HAMAP-Rule:MF_00268};
DE   AltName: Full=Recombinase A {ECO:0000256|ARBA:ARBA00033319, ECO:0000256|HAMAP-Rule:MF_00268};
GN   Name=recA {ECO:0000256|HAMAP-Rule:MF_00268};
GN   ORFNames=IMCC13023_07120 {ECO:0000313|EMBL:EIC92233.1};
OS   Candidatus Aquiluna sp. IMCC13023.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Aquiluna.
OX   NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC92233.1, ECO:0000313|Proteomes:UP000054510};
RN   [1] {ECO:0000313|Proteomes:UP000054510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX   PubMed=22689238; DOI=10.1128/JB.00586-12;
RA   Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT   "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT   member of the Actinobacteria isolated from an arctic fjord.";
RL   J. Bacteriol. 194:3550-3551(2012).
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:0000256|HAMAP-Rule:MF_00268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000256|ARBA:ARBA00009391,
CC       ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU004527}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00268}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIC92233.1}.
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DR   EMBL; AJKR01000002; EIC92233.1; -; Genomic_DNA.
DR   RefSeq; WP_007541357.1; NZ_AJKR01000002.1.
DR   AlphaFoldDB; I0R2Z7; -.
DR   STRING; 1081644.IMCC13023_07120; -.
DR   PATRIC; fig|1081644.3.peg.719; -.
DR   eggNOG; COG0468; Bacteria.
DR   OrthoDB; 9776733at2; -.
DR   Proteomes; UP000054510; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; P-loop containing nucleotide triphosphate hydrolases; 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; IPR049261; RecA-like_C.
DR   InterPro; IPR049428; RecA-like_N.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR023400; RecA_C_sf.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   NCBIfam; TIGR02012; tigrfam_recA; 1.
DR   PANTHER; PTHR45900:SF1; MITOCHONDRIAL DNA REPAIR PROTEIN RECA HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR45900; RECA; 1.
DR   Pfam; PF00154; RecA; 1.
DR   Pfam; PF21096; RecA_C; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54752; RecA protein, C-terminal domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00268}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00268}; Reference proteome {ECO:0000313|Proteomes:UP000054510};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526}.
FT   DOMAIN          37..196
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          201..275
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
SQ   SEQUENCE   362 AA;  38335 MW;  6BC173872CADB55C CRC64;
     MPSASDREKA LDTALAQIDR QFGKGSVMRL GSEERAPIAS ISTGSIALDV ALGIGGLPRG
     RIVEVYGPEA SGKTTIALHA IASAQKAGGT AAFIDAEHAL DPIYAAKLGV DIDALLVSQP
     DTGEQALEIT DMLIRSGSID VIVIDSVAAL VPRAEIEGEM GDTHVGLQAR LMSQALRKLT
     GAISNTDTTA IFINQLREKI GVFFGSPETT SGGKALKFYA SVRLDIRRIE TLKDGQNNAV
     GNRSRVKVVK NKLASPFKQA EFDIIFGEGI SREGSLIDFG VEQDIVNKSG AWYTFDGEQL
     GQGKENSRKF LKENPEIAAT IEQKIKAKLG VGVPRPVADL PVEEIADAVE GTKPVAKAAN
     DA
//
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