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Database: UniProt
Entry: B1CBR0_9FIRM
LinkDB: B1CBR0_9FIRM
Original site: B1CBR0_9FIRM 
ID   B1CBR0_9FIRM            Unreviewed;       353 AA.
AC   B1CBR0;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=Protein RecA {ECO:0000256|ARBA:ARBA00015553, ECO:0000256|HAMAP-Rule:MF_00268};
DE   AltName: Full=Recombinase A {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU000526};
GN   Name=recA {ECO:0000256|HAMAP-Rule:MF_00268,
GN   ECO:0000313|EMBL:EDS71707.1};
GN   ORFNames=ANASTE_01409 {ECO:0000313|EMBL:EDS71707.1};
OS   Anaerofustis stercorihominis DSM 17244.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Anaerofustis.
OX   NCBI_TaxID=445971 {ECO:0000313|EMBL:EDS71707.1, ECO:0000313|Proteomes:UP000005178};
RN   [1] {ECO:0000313|EMBL:EDS71707.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS71707.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244).";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS71707.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS71707.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2008) 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}.
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:EDS71707.1}.
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DR   EMBL; ABIL02000006; EDS71707.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1CBR0; -.
DR   STRING; 445971.ANASTE_01409; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_3_2_9; -.
DR   Proteomes; UP000005178; 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:UP000005178};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526}.
FT   DOMAIN          43..202
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          207..280
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   BINDING         73..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   353 AA;  38011 MW;  4A150F04C862AE5E CRC64;
     MFERKVKVMN PDKEKALELA MRNIESNFGK GAVMKLGDKP AVTIDAISTS SISLDAALGV
     GGLPRGRIIE VYGPESSGKT TVALHVVAEA QKAGGVAAFI DAEHALDPIY AEALGVNIDE
     LIVSQPDTGE QALEITEALV RSAAVDVVVV DSVAALVPKA EIEGDMGDSH VGLQARLMSQ
     ALRKLAGAIN KSNTTAVFIN QLREKVGIMF GNPEVTPGGR ALKFYSSVRL EVRRIDSIKN
     GQEIIGNRTK VKVVKNKVAP PFKIAEFDIM YGKGISREGD IVDMAAKYGI IKKAGAWYSY
     NDEKIGQGRD KAKQFLADNP EIAEHIEKLV LDEVLGRNKE EEPESADTVK AEE
//
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