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Database: UniProt
Entry: A0A0P0DMA8_9MICO
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Original site: A0A0P0DMA8_9MICO 
ID   A0A0P0DMA8_9MICO        Unreviewed;       350 AA.
AC   A0A0P0DMA8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=AOA12_14490 {ECO:0000313|EMBL:ALJ21041.1};
OS   Microbacterium sp. No. 7.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ21041.1, ECO:0000313|Proteomes:UP000059097};
RN   [1] {ECO:0000313|EMBL:ALJ21041.1, ECO:0000313|Proteomes:UP000059097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 7 {ECO:0000313|EMBL:ALJ21041.1,
RC   ECO:0000313|Proteomes:UP000059097};
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete genome sequence of a polypropylene glycol-degrading strain
RT   Microbacterium sp. No. 7.";
RL   Submitted (SEP-2015) 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; CP012697; ALJ21041.1; -; Genomic_DNA.
DR   RefSeq; WP_054684029.1; NZ_CP012697.1.
DR   AlphaFoldDB; A0A0P0DMA8; -.
DR   STRING; 1714373.AOA12_14490; -.
DR   KEGG; mio:AOA12_14490; -.
DR   PATRIC; fig|1714373.3.peg.2977; -.
DR   OrthoDB; 9776733at2; -.
DR   Proteomes; UP000059097; Chromosome.
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:UP000059097};
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..274
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   350 AA;  37426 MW;  56C4065F63EA5ABB CRC64;
     MPSPADREKA LDSALAQIDK QFGKGSVMRL GSDERAPVEV IPTGSIALDV ALGIGGLPRG
     RIVEIYGPES SGKTTLTLHA IANVQRAGGI AAFIDAEHAL DPDYAQKLGV DIDQLLVSQP
     DTGEQALEIA DMLIRSGAID LVVIDSVAAL VPEAEIKGEM GDSHVGLQAR LMSQALRKLT
     GGLNSTKTTA IFINQLREKI GVFFGSPETT AGGKALKFYA SVRLDIRRIE TLKDGTEAVG
     NRTRVKVVKN KMAPPFKQAE FDILYGIGIS REGSLIDFGV EHEIVKKSGS WYTYDGEQLG
     QGKENARSFL ITNDDVAADI EQRIKHKLGI GVPKLVEAPV SDEIAARVSA
//
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