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Database: UniProt
Entry: A0A2Y9AH31_9MICO
LinkDB: A0A2Y9AH31_9MICO
Original site: A0A2Y9AH31_9MICO 
ID   A0A2Y9AH31_9MICO        Unreviewed;       347 AA.
AC   A0A2Y9AH31;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=SAMN05216184_105107 {ECO:0000313|EMBL:SSA41849.1};
OS   Georgenia satyanarayanai.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC   Georgenia.
OX   NCBI_TaxID=860221 {ECO:0000313|EMBL:SSA41849.1, ECO:0000313|Proteomes:UP000250222};
RN   [1] {ECO:0000313|EMBL:SSA41849.1, ECO:0000313|Proteomes:UP000250222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10826 {ECO:0000313|EMBL:SSA41849.1,
RC   ECO:0000313|Proteomes:UP000250222};
RA   Cai Z.;
RL   Submitted (OCT-2016) 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: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}.
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DR   EMBL; UETB01000005; SSA41849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Y9AH31; -.
DR   OrthoDB; 9776733at2; -.
DR   Proteomes; UP000250222; 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:UP000250222};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526}.
FT   DOMAIN          38..197
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          202..275
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   347 AA;  36916 MW;  1BEA56E4CEB3C4D1 CRC64;
     MAAPVADRSK ALEAALSQID RQFGKGSIMR LGDENRPPVA VIPTGSVALD VALGIGGLPR
     GRVVEIYGPE SSGKTTVALH AVANAQRAGG IAAFIDAEHA LDPEYAKKLG VDTDALLVSQ
     PDTGEQALEI MDMLIRSGAL DIVVIDSVAA LVPKAEIEGE MGDSHVGLQA RLMSQALRKI
     TGALSASGTT AIFINQLREK IGVFFGSPET TTGGKALKFY ASVRIDVRRI ETLKEGSDPV
     GNRTRAKIVK NKMAPPFKQA EFDILYGKGI SREGGLLDLG VEHGIVRKSG AWFTYEGDQL
     GQGKENSRRF LKDNPELAVE IEKKILDKLG IGIKAEDATT AEAKVDF
//
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